Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Science for Medicine AM > Learning outcomes > Flashcards

Learning outcomes Flashcards

You may prefer our related Brainscape-certified flashcards:
Biology 101 flashcards
1
Q

Define aetiology

A

Cause of disease

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Define pathogenesis

A

How a disease develops

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Define signs

A

What the doctor sees

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Define symptoms

A

What the patient feels

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Define diagnosis

A

Determining the nature and cause of disease

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Define prognosis

A

A prediction of the probable outcome of the disease

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What are the classifications of disease?

A 
Growth
Unnatural
Degenerative
Developmental
Inflammation
Circulatory
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What proportion of the body’s water is in the ECF and ICF?

A 
ECF= 1/3
ICF= 2/3
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What proportion of ECF is ISF and plasma?

A 
ISF= 80%
Plasma= 20%
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is negative feedback control?

A

A change is detected by receptors, which is then fed to an integration level and compared to a reference level. A difference causes a signal to be sent to an effector and the change is negated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is feed forward control?

A

Changes can be anticipated and negated before they occur

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the first law of thermodynamics?

A

Energy can be converted from one form to another but not created or destroyed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is the second law of thermodynamics?

A

All energy transformations ultimately lead to more entropy in the universe

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

How do cells maintain order if the laws of thermodynamic state they should not?

A

Even though the processes create more ordered, the heat that is released into the environment creates more entropy overall

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Why is equilibrium not reached in biological reaction pathways?

A

Products from one reaction are used in the next reaction in the pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is dynamic steady state?

A

The concentrations are constant but equilibrium is not reached

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Define metabolism

A

The chemical processes in a living organism that allow food to be used for tissue growth

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Define catabolism

A

Releases energy, negative G, spontaneous

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Define anabolism

A

Require energy, positive G, not spontaneous

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What are the uses of ATP and ADP in metabolic processes?

A

Act as free energy carriers, coupling anabolic and catabolic reactions using phosphate group transfers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What are the functions of NADP/NAD and FAD in metabolic processes?

A

Used in reduce reactions as electron carriers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What are the major elements used to construct human biomolecules

A 
O
H
C
N
Na
Cl
K
Ca
S
P
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What is the importance of functional groups?

A

Affect how a molecule acts around others

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What is molecular configuration?

A

The fixed arrangement of atoms in a molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What is molecular conformation?

A

The precise arrangement of atoms in molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What are the 5 types of chemical reactions in the body?

A 
Redox
Making/breaking C-C bonds
Internal rearrangements
Group transfers
Condensation/hydrolysis
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Give an example of a redox reaction in the body

A

Glycolysis in muscles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Give an example of making/breaking C-C bonds in the body

A

Cleavage of glucose in glycolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Give an example of internal rearrangement reactions in the body

A

Glucose-6-phosphate–> fructose-6-phosphate in glycolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Give an example of a group transfer reaction in the body

A

Transfer of phosphate group in glycolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Give an example of a condensation/hydrolysis reaction in the body

A

Formation and breaking of nucleic acids and proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Describe the structures present in all cells

A

Nucleus

Cytoplasm

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

What are the roles of the nucleus in eukaryotic cells?

A

Contains DNA, nucleoprotein and some RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

What is the function of the nucleoli?

A

Sites for ribosomal synthesis and assembly

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

What is the endoplasmic reticulum?

A

Interconnecting network of membranous tubules, vesicles and cisternae

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

What are the two forms of the endoplasmic reticulum?

A

Rough ER

Smooth ER

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

What is the function of the rough endoplasmic reticulum?

A

Synthesises and packages proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

What is the function of the smooth endoplasmic reticulum?

A

Lipid biosynthesis and membrane synthesis and repair

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

What is the function of ribosomes?

A

Protein factories

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

What is the golgi apparatus and its function?

A

Stack of flattened vesicles that package and process secretory proteins and synthesise complex polysaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

What are lysosomes and their function?

A

Membrane bound organelles containing granular materials used to break down bacteria and debris

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

What are peroxisomes and what is their function?

A

Membrane bound organelles containing catalase to regulate hydrogen peroxide concentration and oxidases involved in beta-oxidation of fatty acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

What is the structure of mitochondria?

A

Permeable outer membrane containing porin
Folded inner membrane- cristae
Filled with amorphous matrix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

What is the function of the mitochondria?

A

Powerhouse of the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

What are the components of the cytoskeleton?

A

Microfilaments- fine strands of actin

Microtubules- Larger than microtubules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

What is the role of the cytoskeleton?

A

Provide strength and support

Allow for cell motility

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

What is a hydrogen bond?

A

Electrostatic attraction between polar groups when H is bound to O, N or F

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

What defines a molecule’s water solubility?

A

Polarity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

Define the term amphipathic

A

A molecule containing both hydrophobic and hydrophilic parts

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Give an example of an amphipathic molecule

A

Phospholipids- hydrophilic heads, hydrophobic tails

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

How do amphipathic molecules act in water?

A

Minimise disruption by forming bilayers or micelles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

How can pH be calculated?

A

pH=-log[H=]

pH=pKa=log[A-]/[HA]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

What are buffers?

A

Solutions of weak acids and their salt

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

How do buffer solutions work?

A

If OH- is added, it combines with free H+ to form H2O
If H+ is added, it combines with OH- to form H2O
These ions are then replaced by the dissociation of acid and water and the pH remains constant

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

Describe the basic structure of a cell membrane

A

Phospholipid bilayer containing proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

List the classes of membrane proteins

A

Integral membrane proteins

Peripheral proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

What are integral membrane proteins?

A

Amphipathic proteins that cannot be removed without disrupting the membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

What are the types of integral membrane protein and their functions?

A

Channels, through which ions can cross
Carriers, to transport substances across membranes
Enzymes, with binding sites
Receptors, recognition sites

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

What are peripheral proteins?

A

Non-amphipathic proteins that can be removed without major disruption to the membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

What function do peripheral proteins have?

A

Usually enzymatic

Important for cell shape and motility

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

What is the protein content of different cell membranes?

A

Schwann cells= 18%
Normal= 50%
Mitochondria= 75%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

What factors aid diffusion?

A

Large surface area
High permeability
High concentration gradient

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

What must molecules be to diffuse through the membrane?

A

Small
Uncharged
Hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

What are the different types of channel proteins?

A

Open channels

Gated channels- ligand or voltage gated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

How do voltage gated channels work?

A

Changes in the electrical potential act on charged regions of channel proteins, changing their conformation, opening or closing the channel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
66
Q

How do ligand gated channel proteins work?

A

When a certain chemical binds to a channel protein, it produces a change in conformation, and opens or closes the channel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
67
Q

What is the electrochemical gradient?

A

The difference in charge between two compartments

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
68
Q

What charge is carried by the inside of the cell?

A

-70mV

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
69
Q

What are carrier mediated transport systems?

A

Proteins with binding sites for a substance, that changes conformation upon binding, allowing the molecule to diffuse into the cell, and allowing the protein to return to its original shape

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
70
Q

What are the types of carrier mediated transport systems?

A

Facilitated diffusion

Active transport

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
71
Q

What is active transport?

A

Transport against a concentration gradient, requiring energy from ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
72
Q

Define osmolarity

A

Concentration of a solution, expressed as the total number of osmoles per litre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
73
Q

Define tonicity

A

Concentration of non penetrating solutes on the two sides of the membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
74
Q

What are the 3 types of solutions that can occur in the body?

A

Isotonic
Hypotonic
Hypertonic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
75
Q

What are isotonic solutions?

A

Equal number of non-penetrating cells on either side of the membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
76
Q

What are hypotonic solutions?

A

Solutions where the concentration of non-penetrating particles are higher inside the cell than outside

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
77
Q

What are hypertonic solutions?

A

Solutions where the concentration of non-penetrating cells is higher outside the cell than inside

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
78
Q

Explain the movement of water in and out of the cell in hyper and hypotonic solutions

A 
Hypotonic= water moves into cell
Hypertonic= water moves out of cell
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
79
Q

Describe the process of endocytosis

A

Invagination of the membrane to form a vesicle around the target substance, which eventually separates from the membrane on the cytoplasmic side and migrates into the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
80
Q

Describe the process of exocytosis

A

Invagination of the membrane around the target substance from the cytoplasmic side, which opens out into the extracellular space

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
81
Q

What is epithelial tissue?

A

Tissue that covers surfaces and separates compartments

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
82
Q

What are cell-cell junctions?

A

Junctions created between epithelial cells providing cell anchorage, sealing intracellular spaces and allowing for cell-cell communication

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
83
Q

What are desmosomes?

A

Adhering junctions proving firm anchorage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
84
Q

What are tight junctions and what is their function?

A

Joining of membrane between two cells, forming a virtually impermeable barrier, sealing sections

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
85
Q

What are gap junctions and what are their functions?

A

Connection between cytoplasm of two cells, allowing for cell-cell communication

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
86
Q

What are cell-extracellular matrix junctions called?

A

Hemidesmosomes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
87
Q

What is the function of hemidesmosomes?

A

Anchor cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
88
Q

What are the types of epithelial cells?

A

Squamous
Cuboidal
Columnar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
89
Q

What is the structure and function of simple squamous cells?

A

Thin, single cell, allows for easy diffusion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
90
Q

What is the function of simple cuboidal cells?

A

Secrete, absorption, pumping

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
91
Q

What si the function of ciliated columnar cells?

A

Move mucus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
92
Q

What is the structure of stratified squamous epithelial cells?

A

Multiple layers, thick, layers can be sloughed off to allow for new growth

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
93
Q

What is the function of stratified cuboidal cells?

A

Protection

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
94
Q

What is the function of stratified columnar cells?

A

Protection and secretion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
95
Q

What epithelial cells are in the liver?

A

Hepatocytes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
96
Q

What functions do hepatocytes have?

A

Secretion

Line blood vessels and bile ducts

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
97
Q

How are cells arranged in the kidneys?

A

Arranged into nephrons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
98
Q

What are the functions of the kidney nephrons?

A

Filtration of blood, partial absorption of filtrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
99
Q

What do epithelial cells line in the kidney?

A

Blood vessels and the renal pelvis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
100
Q

What are glands?

A

Collections of multi or single celleular secretory epithelial cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
101
Q

What are the 2 types of glands and where do they secrete into?

A

Endocrine- secrete into bloodstream

Exocrine- secrete onto surface i.e. sweat

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
102
Q

What are the different gland structures?

A

Simple- tubular, acinar

Compound- tubuloacinar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
103
Q

What kind of secretions does each gland type secrete?

A 
Tubular= thin, watery
Acinar= thicker, mucousal
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
104
Q

What are the consequences of abnormal glandular function?

A 
Overproduction= pituitary giantism 
Underproduction= pituitary dwarfism
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
105
Q

What is the extracellular matrix comprised of?

A

Fibres
Ground substance
Tissue fluid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
106
Q

What kind of fibres are present in the extracellular matrix?

A

Collagen fibres

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
107
Q

What are the differences between collagen and elastic fibres?

A

Collagen is flexible bit inelastic

Elastic fibres are very elastic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
108
Q

What is group substance composed of?

A

Proteoglycans
Glycoproteins
Hyaluronic acid
Water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
109
Q

What are the three layers of the skin?

A

Epidermis
Dermis
Hypodermis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
110
Q

What are the 5 layers of the epidermis?

A 
Stratum basale
Stratum spinosum
Stratum gramulosum
Stratum lucidium
Stratum corneum
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
111
Q

How does the stratum basale bind?

A

To the basement membrane via hemidesmosomes

To other cells via desmosomes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
112
Q

How is the stream granulosum defines?

A

Presence of keratohyalin granules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
113
Q

What is the turnover rate of the strum corneum?

A

30 days

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
114
Q

What 2 layers is the dermis composed of?

A

Papillary layer

Reticular layer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
115
Q

What is the papillary layer of the dermis composed of?

A

Loose connective tissue
Blood vessels
Nerve endings

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
116
Q

What is the reticular layer of the dermis composed of?

A

Sense irregular connective tissue
Collagen bundles
Elastic fibres

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
117
Q

What is the interface between the dermis and epidermis like?

A

Irregular

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
118
Q

What are the functions of bone?

A

Mechanical support and attachment for muscles, tendons, ligaments and joints
Protects internal organs
Mineral reservoir
Support blood formation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
119
Q

Describe the process of endochondral ossification

A

Bone forms as cartilage first
Blood vessels and osteogenic cells invade the cartilage framework
Cartilage remains as growth plates until 18-21 years old

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
120
Q

Describe the process of intramembranous ossification

A

Bone forms as a fibrous plate

Bone cells differentiate from fibroblasts and haematopoietic precursors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
121
Q

What is the composition of bone?

A

20% water
35% proteins- collagen type 1, growth factor proteins, other matrix proteins
Minerals

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
122
Q

What are the 3 areas of long bone and where are they found?

A

Epiphyses- end of a bone
Metaphyses- between the two
Diaphyses- shaft of bone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
123
Q

What is the epiphyses of long bone made up of and why?

A

Trabecular (spongey) bone

Act as a softer interface at joints

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
124
Q

What is the diaphyses of bone composed of?

A

Cortical bone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
125
Q

What is cortical bone of the diaphyses in long bone arranged into and why?

A

Haversian canals

Gives bone strength

126
Q

What are osteoclasts?

A

Bone reabsorbing cells

127
Q

What are osteoblasts?

A

Cells that lay down more bone

128
Q

What are osteocytes?

A

Sensors of mechanical pressure and damage

129
Q

What are the 4 classes of amino acids?

A

Acidic
Basic
Polar
Nonpolar

130
Q

What are the functions of proteins in the body?

A 
Movement
Protection
Transport
Enzymes
Receptors
Structural
Storage
Hormones
Control of gene expression
131
Q

What is the primary structure of proteins?

A

Sequence of amino acids linked by peptide bonds

Beads on a string structure

132
Q

What is the secondary structure of proteins?

A

A level of protein folding involving hydrogen bonds between amino acid residues that are close together into either alpha helices or beta pleated sheet

133
Q

What bonds hold together the alpha helix?

A

H bonds between N-H and the C=O groups

134
Q

What is the tertiary structure of proteins?

A

A level of protein folding involving amino acid residues that are far apart in the linear sequence

135
Q

What bonds can form in the tertiary structure of proteins?

A 
Van der Waals
Ionic interactions
Hydrogen bonds
Sysulphide bridges
Hydrophobic interactions
136
Q

What is the quaternary structure of proteins?

A

Joining of protein and prosthetic subunits

137
Q

What is an enzyme cofactor?

A

A non protein component needed for activity

138
Q

What is a prosthetic group of an enzyme?

A

Covalently bonded cofactor

139
Q

What is an apoenzyme?

A

The protein component of an enzyme containing a prosthetic group

140
Q

How do enzymes catalyse reactions?

A

Increase rates of spontaneous reactions
Lower activation energy
Accelerate movement towards equilibrium

141
Q

What is the Michaelis constant and how is it calculated?

A

Km- the concentration of the substrate that catalyses the associated reaction at half of the maximum rate
Vmax (max rate of reaction) / 2

142
Q

What does a high Km mean?

A

Low enzyme affinity

143
Q

What does a low Km mean?

A

High enzyme affinity, faster reaction

144
Q

How do competitive inhibitors work?

A

Non-covalently bind to enzymes in the same way the intended substrate does

145
Q

How do non-competitive inhibitors work?

A

Non-covalently bind to a site other than the active site and change the shape of the active site

146
Q

Explain the concerted model of allosteric enzymes

A

Each subunit can flip between conformations with a high and a low Km
When one substrate binds, it increases the affinity of all other subunits for the substrate

147
Q

Explain the sequential model of allosteric enzymes

A

Binding causes a change in one subunit, causing a change in another to make further binding easier

148
Q

What are the major carbohydrates in the diet?

A

Monosaccharides- glucose, galactose, fructose

Disaccharises- maltose, sucrose, lactose

149
Q

What is the difference between Glucokinase and hexokinase?

A 
Glucokinase= high Vmax, which Km
Hexokinase= low Vmax, low Km
150
Q

Where is glucokinase found and how does it work?

A

Liver
High Vmax and Km mean it only picks up glucose when the concentration is high, but it does so quickly, meaning as much glucose is trapped in the liver as possible

151
Q

Where is hexokinase found and how does it work?

A

Tissues

Can bind to glucose even at low concentrations and means tissues are easily satisfied

152
Q

What is glycogen?

A

A polymer of glucose with (alpha 1–>4) linked subunits and an (alpha1–>6) branch every 8-12 residues

153
Q

How is glycogen synthesised?

A

Glucogenin covalently binds glucose from UDP-glucose to form chains of approx 8 subunits
Glycogen synthase then takes over and extends the chains until they are broken by glycogen branching enzyme to form the branching points

154
Q

How is glycogen degraded?

A

Glucose subunits are removed from the ends of the branches one at a time as G-1-P

155
Q

What are the 2 phases of glycolysis?

A

Preparatory

Payoff

156
Q

What are the 10 steps of glycolysis?

A
  1. Phosphorylation of glucose
  2. Conversion of G-6-P to F-6-P
  3. Phosphorylation of F-6-P to F-1,6-bisP
  4. Cleavage of F-1,6-bisP
  5. Interconversion of triose sugars
  6. Oxidation of G-3-P to 1,3-bisPG
  7. P transfer from 1,3-bisPG to ADP
  8. Conversion of 3-PG to 2-PG
  9. Dehydration of 2-PG to PEP
  10. Transfer of P from PEP to ADP
157
Q

What catalyst is involved in phosphorylation of glucose, what is needed for the reaction to take place and is the ΔG positive or negative?

A

Hexokinase
1 ATP
Negative ΔG

158
Q

What catalyst is involved in the conversion of G6P to F6P and is the ΔG positive or negative?

A

Phosphohexose isomerase

Positive, but very low, ΔG

159
Q

What catalyst is involved in phosphorylation of F6P to F1,6bisP, what is needed for the reaction to take place and is the ΔG positive or negative?

A

Phosphofructokinase
1ATP
Negative ΔG

160
Q

What catalyst is involved in the cleavage of F1,6bisP and is the ΔG positive or negative?

A

F1,6bisP aldolase

Positive ΔG

161
Q

What catalyst is involved in the interconversion of triode sugars and is the ΔG positive or negative?

A

Triose phosphate isomerase

Positive ΔG

162
Q

What catalyst is involved in the oxidation of G3P to 1,3bisPG, is the ΔG positive or negative and what is produced?

A

Glyceraldehyde 3-phosphate dehydrogenase
Positive ΔG
2 NADH produced

163
Q

What catalyst is involved in the P transfer from 1,3bisP to ADP, is the ΔG positive or negative and what is produced?

A

Phosphoglycerate kinase
Negative ΔG
2 ATP produced

164
Q

What catalyst is involved in the conversion of 3PG to 2PG and is the ΔG positive or negative?

A

Phosphoglycerate mutase

Positive, but very low, ΔG

165
Q

What catalyst is involved in the dehydration of 2PG to PEP and is the ΔG positive or negative?

A

Enolase

Positive ΔG

166
Q

What catalyst is involved in the transfer of P from PEP to ADP, is the ΔG positive or negative and what is produced?

A

Pyruvate kinase
Very negative ΔG
2 ATP and pyruvate produced

167
Q

What is gained per molecule of glucose invested in glycolysis?

A

2ATP and 2 pyruvate

168
Q

What is the function of gluconeogenesis?

A

Convert pyruvate back into glucose

169
Q

What reactions are catalysed by lactate dehydrogenase?

A

Interconversion of lactate and pyruvate

170
Q

What reactions are catalysed by pyruvate dehydrogenase?

A

Interconversion of pyruvate and acetyl coA

171
Q

What is the fate of blood lactate?

A

Lactate is transported to the lover in the blood and converted back to glucose using gluconeogenesis

172
Q

What is the cori cycle?

A

The cycle between glycolysis and gluconeogenesis

173
Q

How many bypass reactions are in gluconeogenesis and how many are reverse reactions?

A

4 bypass reactions

7 reverse reactions

174
Q

What is the fate of absorbed galactose?

A

Joins glycolysis through conversion to G1P by UDP. This is then converted to G6P to enter glycolysis

175
Q

What is the fate of absorbed fructose?

A

Forms F1P through phosphorylation, then glyceraldehyde, then G3P to join glycolysis

176
Q

What is the pentose phosphate pathway?

A

Cycle producing NADPH and pentose sugars needed for nucleic acid synthesis

177
Q

What are the phases of the posts phosphate pathway?

A

Oxidative, irreversible

Non-oxidative, reversible

178
Q

What happens in the oxidative, irreversible part of the pentose phosphate pathway?

A

G6P is converted to a pentose phosphate

NADPH generated

179
Q

What happens in the non-oxidative, reversible part of the pentose phosphate pathway?

A

G6P is interconverted with various 3,4,5,6 and 7 carbon sugars

180
Q

What is an x-ray?

A

Electromagnetic packet of energy with wavelength between 0.1 and 10 nanometres

181
Q

Briefly describe how an X-ray works?

A

High energy electrons are fired at a heavy atom material
The collision of the electrons and heavy materials creates braking radiation in the form of x-rays
The x-rays are then directed at the target and some rays are absorbed and some pass through and hit the imaging film, creating the image

182
Q

What has the least to the most absorption of x-rays?

A

Air
Fat
Muscle
Bone

183
Q

How do ultrasounds work and what are they used to image?

A

Firing sonic waves with frequencies between 2 and 18 megaHertz into the patient
Soft tissues and embryonic development

184
Q

How does a CT scan work and what is it most commonly used for?

A

Taking a series of 2D x-rays around an axis of rotation to create a 3D image
Head

185
Q

What is fluoroscopy?

A

Imaging technique used to obtain real time moving images of the internal structures of the body

186
Q

What is iodinated contrast media?

A

IV radiocontrast containing iodine which enhances the visibility of vascular structures and organs during radiographic procedures

187
Q

What is barium used for in x-rays?

A

Absorbs x-ray photons, helping to outline the GI tract

188
Q

Where does the citric acid cycle occur?

A

Mitochondril matrix

189
Q

What do pyruvate and fatty acids form to enter the civic acid cycle?

A

Acetyl coA

190
Q

What is produced from every turn of the citric acid cycle?

A

3 NADH
2 CO2
1 FADH2
1 GTP

191
Q

What is the final stage of respiration and where does it take place?

A

Electron transport chain

Mitochondrial matrix and intramembranous space

192
Q

What proteins are involved in the electron transport chain?

A

NADH-Q oxidoreductase
Succinate Q reductase
Q cytochrome C oxireductase
Cytochrome C oxidase

193
Q

What is the function of NADH Q oxidoreductase in the electron transport chain?

A

Reduce NADH and pass electrons to uboquinone

Pump H+ ions into intramembranous space

194
Q

What is the function of succinate Q reductase in the electron transport chain?

A

Reduces FADH2 and passes electron to ubiquinone

195
Q

What is the function of Q cytochrome C oxidoreductase in the electron transport chain?

A

Passes electrons from ubiquinol to cytochrome C

Pumps H+ ions into intramembranous space

196
Q

What is the function of cytochrome C oxidase?

A

Pass electrons from cytochrome C to oxygen

Pump H+ ions into intramembranous space

197
Q

What is the function of pumping H+ ions across the inner mitochondrial membrane?

A

Create a proton gradient so the protons can diffuse back through into the matrix, turning ATP synthase

198
Q

Describe the process by which H+ ions pass through the inner mitochondrial membrane

A

As the protons passively diffuse the membrane, ATP synthase turns, yielding energy to bind ADP and Pi

199
Q

How many turns of ATP synthase are needed to bind ADP and Pi?

A

3

200
Q

What are the functions of lipids?

A 
Store energy
Structural component of cell membranes
Enzyme cofactor
Hormones
Synthesis of vitamins A,D,E and K
Signalling molecules
201
Q

What are the major lipid classes?

A

Fatty acids
Triacylglycerides
Phospholipids

202
Q

What is the structure of a fatty acid?

A

Hydrocarbon chain with carboxylic acid at one end

203
Q

What are the categories of fatty acids?

A

Essential
Good
Bad
Really bad

204
Q

What are essential fatty acids?

A

Fatty acids cannot we must ingest as we cannot synthesise them- we cannot synthesise carbon double bonds past carbon 9

205
Q

What are good fatty acids?

A

Fatty acids high in polyunsaturated fat

206
Q

What are bad fatty acids?

A

Fatty acids high in saturated fat

207
Q

What are really bad fatty acids?

A

Trans fatty acids

208
Q

What are triacylglycerols?

A

Esters of fatty acids and glycerol

209
Q

What are the functions of triacylglycerols?

A

Major component of adipose tissue- act as insulation and dietary fuel

210
Q

What are phospholipids?

A

Glycerol with two fatty acid tails an a phosphate group head

211
Q

What is the function of phospholipids?

A

Form the basic structure of the cell membrane

212
Q

How are triacylglycerols digested?

A

Through pancreatic enzymes in the small intestine

Emulsion by bile salts and peristalsis

213
Q

What are triacylglycerols digested by and into?

A

Pancreatic lipase into monoacylglycerols and two fatty acids

214
Q

What are cholesterol esters broken down into?

A

Cholesterol and fatty acids

215
Q

What are phospholipids broken down into?

A

Lysophospholipids and fatty acids

216
Q

How are fatty acids transported round the body?

A

Fatty acids and cholesterol esters into chylomicrons which are released into the bloodstream

217
Q

What happens when chylomicrons reach the tissues?

A

Hydrolysed to fatty acids and glycerol for uptake into the cell, for energy or storage

218
Q

How are free fatty acids transported in the blood?

A

In a complex with serum albumin

219
Q

Explain How fats are transported in high and low density lipoproteins

A 
LDL= fat from liver to tissues
HDL= fat from tissue to liver for elimination
220
Q

What is the beta oxidation pathway and where does it occur?

A

Degratation of fatty acids 2 carbons at a time

Mitochondrial matrix

221
Q

What are the 3 stages of the beta oxidation pathway?

A

Activation
Transport
Degradation

222
Q

What happens in the first step of the beta oxidation pathway?

A

Fatty acids are activated to form fatty acylcoA in the cytoplasm
2 ATP used

223
Q

What happens in the second step of the beta oxidation pathway?

A

Carnitine shuttle transfers long chain fatty acyl coA to the inside of the mitochondrion

224
Q

What happens in the third stage of the beta oxidation pathway?

A

Fatty acyl coA is dehydrogenated to form FADH and an intermediate
The intermediate is then hydrated
The resulting intermediate is then dehydrogenated to give NADH and an intermediate
Thiolysis forms acetyl coA to feed into citric acid cycle

225
Q

What is formed in fatty acid synthesis?

A

Acetyl coA
FADH
NADH
Carbon species 2 Cs shorter than original fatty acid

226
Q

What are ketone bodies?

A

Fuel sources synthesised from acetyl coA that can fuek the brain, unlike fatty acids

227
Q

Where does ketogenesis occur?

A

Liver

228
Q

What are the main nitrogen containing molecules in the body?

A

Amino acids
Ammonia
Urea

229
Q

What are the 3 types of protein digestion?

A

Gastric
Pancreatic
Intestinal

230
Q

How are proteins digested in the stomach?

A

Denaturation of proteins males them more susceptible to actions of pepsin

231
Q

How are proteins digested by the pancreas?

A

Pancreatic enzymes create a mix of free amino acids and short peptides around 2-8 units in length

232
Q

How are proteins absorbed in the intestines?

A

Free amino acids absorbed into the portal system

Di and tripeptides are absorbed and broken down to free amino acids in enterocytes of the brush border

233
Q

What is different about glutamate compared to the other amino acids?

A

Can obtain its nitrogen from ammonia rather than preexisting amino acids through transaminase reactions

234
Q

Describe the catabolism of protein

A

Once the proteins are broken down, they are deaminated and catabolised into intermediated of the citric acid cycle and glycolysis to be used as energy

235
Q

How is nitrogen transported from the muscles to the liver?

A

Through the bloodstream as alanine

236
Q

What happens to amino acids once in the liver?

A

Built up to form glucose, creating ammonia and urea and requiring the use of transferase enzymes

237
Q

How is urea formed?

A

From ammonia in the urea cycle

238
Q

How is ammonia formed?

A

Through oxidative deamination, where glutamate loses its nitrogen as ammonia

239
Q

How is the nervous system organised?

A

Brain
Spinal cord
Peripheral nerves

240
Q

How is the peripheral nervous system organised?

A

Autonomic- sympathetic and parasympathetic

Somatic

241
Q

Describe the general structure of neuron

A

Cell body- contains nucleus
Dendrites- route to other neurons
Axon- carries action potential
Terminals- connects with nerves/muscles

242
Q

What is the resting membrane potential?

A

-70mV

243
Q

How is the resting membrane potential created?

A

Na/K pumps pump K into cell and Na out
K channels allow K to leak out of cell via facilitated diffusion
There are therefore more positive ions outside the cell than inside the cell, creating the membrane potential

244
Q

What are action potentials?

A

All or nothing signals that either fire a potential of +40mV or nothing
Intensity is shown in frequency, not amplitude

245
Q

What are graded potentials?

A

Potentials that vary in intensity with the intensity of the stimulus
Can be depolarising or hyperpolarising
Can summate

246
Q

How are nerve signals fired?

A

Once a graded potential reaches threshold, an action potential will be fired
This changes the potential of the neutron to +40mV, where the Na channels open and depolarise the cell
This then opens K channels, depolarising the cell
Na/K pump restores resting membrane potential

247
Q

What are the 3 types of nerve fibres?

A

Afferent
Interneurones
Efferent

248
Q

What is the function of the 3 types of neuron?

A 
Afferent= detect changes or sensory stimuli
Interneurones= Carry signal to brain
Efferent= carry signals to effector tissues or muscles
249
Q

How does axon size affect transmission speed?

A

Larger axon=faster transmission

Resistance is decreased, allowing the charge to travel further and reducing the time needed

250
Q

How does myelination affect transmission speed?

A

Myelnation=faster transmission

Transmission can travel further due to insulation provided

251
Q

What is the neuromuscular junction and its structure?

A

Junction between the nerve and effects muscle
Synapse between the two
Muscular side has sarcolemma

252
Q

Describe the process of neuromuscular transmission

A

Action potential opens Ca- channels in presynaptic terminal
Triggers fusion of vesicle and acetylcholine released into cleft
Diffused across synapse and binds to receptors in junctional folds
End plate potential reached and action potential fired
Each removed from cleft by acetycholinesterase

253
Q

What are the main differences between neuron-neuron junction and neuromuscular junction?

A

Neuron-neuron= wide range of neurotransmitters, range of postsynaptic potentials, different anatomical arrangement, synaptic connectivity

254
Q

What is the structure of skeletal muscle?

A

Multinucleated striated fibres collected in bundles and wrapped in sheathes

255
Q

How do muscles contract?

A

Calcium ions bind to troponin on the actin filament and remove the tropomyosin, exposing the actin binding sites
The myosin converts an attached ATP to ADP and Pi and used this energy too bind to the actin
The myosin head then releases the ADP and unattaches
When Ca ions return to the sarcoplasmic reticulum, the tropomyosin again binds and the contraction stops

256
Q

What is an isotonic muscle twitch?

A

Contraction with shortening length

257
Q

What is an isomeric muscle twitch?

A

Contraction with constant length

258
Q

What is tetanus?

A

State of extended contraction via the summation of action potentials
no respite in which Ca can return to sarcoplasmic reticulum

259
Q

What is fatigue?

A

State caused by repeated muscle stimulation

260
Q

What is the purpose of fatigue?

A

Prevents using vast quantities of ATP

261
Q

What are oxidative fibres?

A

muscle fibres with more mitochondria and myoglobin

262
Q

What are glycolytic fibres?

A

Muscle fibres with few mitochondria and a high concentration of glycolytic enzymes and glycogen

263
Q

What is the structure of smooth muscle?

A

Mononucleate non striated spindles

Diagonally arranged actin and myosin filaments

264
Q

What are receptors?

A

Proteins that recognise a specific compound or molecule

265
Q

What are agonists and antagonists?

A

Agonists mimic the effect of a receptor

Antagonists block the normal action of a recteptor

266
Q

Define the term affinity of a drug for a receptor

A

The strength of the chemical attraction between the drug and the receptor

267
Q

What is the efficacy of an agonist?

A

How good an agonist is at activating a specific receptor

268
Q

In what ways can receptors pass signals across the membrane?

A

Receptors that act as ion channels, interact with JAK kinases or G proteins, or have intrinsic enzyme activity

269
Q

What are the types of G protein receptor and how do they work?

A

Adenylyl cyclase- change concentration of cAMP to activate or inactivate PKA
Phospholipase C- produce diacylglycerol and inositol triphosphate to activate PKC and release internal Ca-

270
Q

What are the sources of intracellular calcium?

A

From internal stores
From transport via ligand or voltage gated channels into the cell
Via inhibition of Ca- transport out of the cell

271
Q

What is the structure of cutaneous sensory receptors?

A

Nerve ending protected by capsule

Stretch sensitive ion channels- present in distal tip of axon or in specialised sensory cells

272
Q

How do cutaneous sensory receptors transmit a singal?

A

Stretch sensitive ion channels are activated, releasing a neurotransmitter to create a generator potential in the dendrites

273
Q

Describe the concept of frequency coding

A

The bigger the stimulus, the greater the receptor potential and the higher frequency of action potentials

274
Q

What are muscle spindles?

A

Intrafusal fibres that monitor muscle length and they way in which they contract

275
Q

What is the structure of muscle spindles?

A

Intrafusal fibres containing sarcomeres, controlled by gamamotoneurones

276
Q

What is the function of the golgi tendon organs?

A

Monitor muscle tension

277
Q

How is muscle tension monitored?

A

The stretch in tendons- monitored by nerve endings- is directly related to muscle tension

278
Q

Describe the stretch reflex

A

A sharp tap to the tendons, which are inelastic- so the force is transferred to the muscle which stretch and stimulate the spindles, activating alphamotorneurons and stimulating the agonist to contract

279
Q

Describe the clasp knife reflex

A

As the muscle contracts, it pulls on tendons and the golgi tendon organs increase their discharge, activating inhibiting neurons to the agonist, decreasing contraction strength and activating the antagonist muscles

280
Q

Describe the flexor-withdrawal reflex

A

Sensory stimulus from the nocireceptors causes an increase in the activity of flexor muscles via excitatory interneurons, and decreasing activity in antagonists via inhibitory neurons

281
Q

What is important in the flexor-withdrawal reflex in the legs?

A

If one leg withdraws, the other must extend

Excitatory interneurons crossing the spinal column, activating extensors and inhibiting flexion

282
Q

Where does sympathetic and parasympathetic outflow originate from?

A

Sympathetics- thoracic-lumbar T1-L2

Parasympathetic- Cranial sacral C3-5 and S1-5

283
Q

What is the structure of sympathetic fibres?

A

Short preganglionic fibres, synapse in the sympathetic trunk, long postganglionic fibre

284
Q

What is the structure of parasympathetic fibres?

A

Long preganglionic fibre, with synapse close to or in target organ

285
Q

What neurotransmitters are used by sympathetic and parasympathetic fibres and what receptors do they act on?

A

All preganglionic release acetylcholine onto nicotinic receptors
Sympathetic postganglionic- noradrenaline on alpha or beta receptors
Parasympathetic postganglionic- acetylcholine onto muscarinic

286
Q

What is the average circulating volume of an adult male?

A

5 litres- 1 in lungs, 3 in veins, 1 in heart and arteries

287
Q

What are the functions of blood?

A 
Carraige of physiologically active compounds
Clotting
Defence
Carriage of gas
Thermoregulation
Maintenance of ECF pH
288
Q

What are the 3 plasma proteins?

A

Albumin
Globulins
Fibrinogen

289
Q

What is oncotic pressure?

A

Concentration gradient of plasma proteins that draws water into the circulatory system

290
Q

What is the structure and function of red blood cells?

A

Flexible, biconcave and non-nucleated

Carry oxygen around the body in the blood

291
Q

What is erythropoiesis?

A

The differentiation of pluripotent into erythroblasts, accelerate by erythropoietin

292
Q

What are the 5 main types of white blood cells?

A 
Neutrophils
Eosinophils
Basophils
Monocytes
Lymphocytes
293
Q

What are neutrophils?

A

Phagocytic white blood cells that deal with bacterial infection

294
Q

What are eosinophils?

A

White blood cells that attach pathogens too large for other leukocytes

295
Q

What are basophils?

A

White blood cells that release histamine and heparin to promote inflammation

296
Q

What are monocytes?

A

White blood cells that migrate to tissues and become macrophages

297
Q

What are lymphocytes?

A

White blood cells that can either form B or T cells

298
Q

What factors control white cell formation?

A

Cytokines- growth stimulating factors, interleukins

299
Q

What are platelets?

A

Membrane bound fragments of megakaryocytes

300
Q

What is the function of platelets?

A

Adhere to damaged capillary walls and exposed connective tissue to mediate blood clotting

301
Q

What is haematocrit?

A

Proportion of red blood cells in the blood

302
Q

What is blood viscosity?

A

Thickness of the blood in comparison to water- plasma is 1.8x thicker, whole blood is 3-4x thicker

303
Q

What are the major cells involving innate immunity?

A

Macrophages

Neutrophils

304
Q

What are the major cells involved in adaptive immunity?

A

Lymphocytes

305
Q

What is the role of the innate immune system?

A

Act as the body’s first line of defence

306
Q

What factors are involves in the innate immune system?

A

Physical barriers
Phagocytic cells
Soluble factors

307
Q

What is the process of phagocytosis?

A

Foreign matter is internalised by cytoplasmic vesicles

Matter is digested by lysosomes which contain enzymes

308
Q

What are the primary and secondary lymphoid organs?

A

Primary- where lymphocytes are created, thymus, bone marrow, foetal liver
Secondary- where immune responses are initiated and lymphocytes maintained, lymph nodes, spleen

309
Q

What are the fundamental properties of the adaptive immune response?

A

Specificity
Diversity
Memory
Recruitment of other defence mechanisms

310
Q

What is the role of B lymphocytes?

A

Form plasma cells

Synthesise antibodies

311
Q

What is the structure and function of an antibody?

A

Y shaped protein
paratope= antigen binding region
Coat surface of antigen to prevent entry to cell, stimulate other parts to the immune system, opsonisation

312
Q

What is the complement system?

A

System made of 25 serum proteins that can cause

  • recruitment of inflammatory cells
  • opsonisation of bacteria
  • lysis of bacteria

Science for Medicine AM (1 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions