Overview of Science for Medicine Flashcards

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1
Q

What is aetiology?

A

The cause of the disease

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2
Q

What is pathogenesis?

A

How the disease develops

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3
Q

What is a sign?

A

What the doctor sees

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4
Q

What is a symptom?

A

What the patient experiences and tells you

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5
Q

What is a diagnosis?

A

Determining the nature and cause of disease or injury

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6
Q

What is a prognosis?

A

A prediction of the probable outcome of the disease

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7
Q

What are the 6 classifications of disease?

A
Growth 
Inflammation
Degenerative 
Developmental 
Circulatory 
Unnatural
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8
Q

What percentage of ECF is ISF?

A

80%

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9
Q

What percentage of ECF is plasma?

A

20%

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10
Q

What is negative feedback?

A

When a change to the system is detected and the feedback works to counteract this change and restore the system back to normal

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11
Q

Why is the feed forward system more sophisticated?

A

Because the changes can be anticipated before the significant changes have happened

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12
Q

What fraction of body water is in the ECF?

A

1/3

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13
Q

What fraction of body water is in the ICF?

A

2/3

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14
Q

Can energy be destroyed?

A

No energy can be converted from one form to another but cannot be created or destroyed

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15
Q

What do all energy transformations lead to?

A

An increase in disorder in the system

An increase in entropy

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16
Q

Why is it unusual that there is an increase in entropy for cells?

A

Because cells create order

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17
Q

What do cellular processes release that creates more disorder in the system?

A

Heat

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18
Q

What is metabolism?

A

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

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19
Q

What is metabolism a mix of?

A

Summative and degradative reactions

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20
Q

What is another name for degradative reaction?

A

Catabolism

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21
Q

What is another name for summative reactions?

A

Anabolism

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22
Q

Do catabolic reactions have a positive or negative ve?

A

Negative

-ve

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23
Q

Do anabolic reactions have a positive or negative ve?

A

Positive

+ve

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24
Q

What is the energy obtained from catabolic reactions used for?

A

It is used up in anabolic reactions to produce more highly ordered compounds

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25
Q

What is the general function of NADP, NAD and FAD?

A

They are use in redox reactions as electron carriers

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26
Q

What do ATP and ADP act as?

A

Free energy carriers, that couple anabolic and catabolic reactions

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27
Q

How does ATP/ADP couple anabolic and catabolic reactions together?

A

Using phosphate group transfers

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28
Q

What are the major elements used to construct human biomolecules?

A
Oxygen
Carbon 
Hydrogen 
Nitrogen 
Sulphur 
Phosphate
Sodium 
Potassium 
Chlorine 
Calcium
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29
Q

What is meant by cis?

A

Functional groups on the same side

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30
Q

What is meant by trans?

A

Functional groups on opposite sides

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31
Q

Why are functional groups on molecules so important?

A

They affect the interactions of that molecule with other molecules

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32
Q

What is the configuration of a molecule?

A

The fixed arrangement of atoms in a molecule

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33
Q

What is the conformation of a molecule?

A

The precise arrangement of atoms in a molecules

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34
Q

What are the 5 chemical reactions that occur in living organisms?

A
Redox
Making/breaking C bonds 
Group transfers 
Condensation/Hydrolysis
Internal Rearrangements
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35
Q

Describe redox reactions

A

When electrons are gained and lost in reduction and oxidation reactions

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36
Q

Usually how many electrons are gained or lost in redox reactions?

A

2

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37
Q

What is an internal rearrangement reaction?

A

When the molecule is rearranged to give it different properties and a different structure

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38
Q

What is a group transfer reaction?

A

When a functional group is transferred from one molecule to another

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39
Q

What is a condensation reaction?

A

The joining together or monomers or molecules usually yielding water

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40
Q

What is a hydrolysis reaction?

A

The breaking down/separation of joined together molecules sing water

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41
Q

What 2 compartments are cells divided into?

A

Nucleus

Cytoplasm

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42
Q

What is the cytosol?

A

The organelles and the fluid

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43
Q

What does the nucleus contain?

A

DNA, nucleoproteins and some RNA

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44
Q

What do the nucleoli serve as sites for?

A

Ribosomal RNA synthesis and Ribosomal assembly

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45
Q

What is the function of rough ER?

A

Synthesises and secretes/packages proteins

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46
Q

Why does rough ER have a studded appearance?

A

Due to the presence of ribosomes

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47
Q

What is smooth ER responsible for?

A

Lipid biosynthesis

Membrane synthesis and repair

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48
Q

What is the function of ribosomes?

A

They carry out protein synthesis

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49
Q

What is the function of the golgi apparatus?

A

To package and process secretory proteins

Also synthesis complex polysaccharides

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50
Q

What does a lysosome contain?

A

Powerful digestive enzymes

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51
Q

What do lysosomes act as?

A

Cellular stomachs

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52
Q

What is the folded inner membrane of mitochondria known as?

A

Cristae

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53
Q

What is mitochondria vital for?

A

Energy production
Citric Acid cycle
Electron transport chain

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54
Q

Are mitochondria mobile cells?

A

Yes

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55
Q

What is the role of the cytoskeleton?

A

Provides strength and support while also allowing for cell motility

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56
Q

What do microfilaments form that line the small intestine?

A

Microvilli

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57
Q

What do microtubules form that line the respiratory tract>

A

Cilia

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58
Q

What structure do microtubules form that are useful during cell division?

A

Spindle fibres

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59
Q

Why is water a polar molecule?

A

Due to the difference in E.N between oxygen and hydrogen

The oxygen is particularly E.N

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60
Q

Between what elements does H bonding occur?

A

H-F
H-O
H-N

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61
Q

Are molecules that form H bonds water soluble?

A

Yes

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62
Q

When a water soluble compound is added to water what are the water-water bonds replaced by?

A

Water-solute

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63
Q

Are uncharged molecules soluble?

A

No

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64
Q

How do uncharged molecules arrange themselves in water?

A

They form cages

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65
Q

Why do uncharged molecules form cages?

A

To minimise disruption of the surrounding water molecules

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66
Q

What is meant by the term amphipathic?

A

The molecules contains both hydrophobic and hydrophilic parts

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67
Q

Give an example of an amphipathic molecule

A

Phospholipids
Have hydrophilic head
Have hydrophobic tail

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68
Q

What is pH a measure of?

A

H+ conc.

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69
Q

What equation measures pH?

A

pH -log(H+)

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70
Q

What is a buffer a solution of?

A

A weak acid

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71
Q

What happens to strong acids in solution?

A

They fully dissociate

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72
Q

Why is it that weak acids can only form buffers?

A

Because they are only partially dissociated meaning they can dissociate more and less to compensate for the disrupted pH

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73
Q

What happens to weak acids in solution?

A

They do no dissociate very much

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74
Q

What is the cell membrane made up of?

A

A phospholipid bi-layer

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75
Q

How would you describe the permeability of the cell membrane?

A

Selectively permeable

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76
Q

Can permeability of the cell membrane vary?

A

Yes depending on the needs of that cell at that time

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77
Q

Why is the cell membrane very flexible?

A

Due to fatty acids

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78
Q

What does the membrane provide binding sites for?

A

Chemical recognition

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79
Q

What are the 2 classes of membrane proteins?

A

Integral membrane proteins

Peripheral proteins

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80
Q

Why are integral proteins amphipathic?

A

Because they span the full membrane which is also amphipathic

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81
Q

How do integral proteins act as channels?

A

They create a passage for which ions can cross the membrane

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82
Q

How do integral proteins act as carriers?

A

They transport substances across membranes acting like pumps

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83
Q

How do integral enzymes act as carriers?

A

They create binding sites at the surface which interact with intercellular pathways

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84
Q

How do integral enzymes act as receptors?

A

They act as recognition sites for chemicals and signals

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85
Q

What % protein content do mitochondria have?

A

Around 75%

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86
Q

What % protein content do schwann cels have?

A

18%

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87
Q

What % protein content do most cells have?

A

Around 50%

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88
Q

Are peripheral proteins amphipathic?

A

No

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89
Q

From what side do peripheral proteins make contact with the plasma membrane?

A

From the intercellular side

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90
Q

What is meant by diffusion?

A

When molecules spread out from an area of high concentration to an area of low concentration - when the membrane is permeable to the molecule

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91
Q

To diffuse through the lipid bilayer what do molecules need to be?

A

Small
Uncharged
Hydrophobic - lipophilic

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92
Q

What type of membrane channel does water flow through?

A

Aquaporin

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93
Q

What is a voltage gated channel?

A

One which will change conformation in response to a change in electrical potential

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94
Q

What is a ligand gated channel?

A

One which will change conformation in response to a ligand binding

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95
Q

What charge does the inside of the cell have in relation to the outside of the cell?

A

negative

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96
Q

What is facilitated diffusion?

A

Transports of solutes down their conc. gradient requires a change in conformation but needs no direct energy source

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97
Q

What is active transport?

A

When energy is require to move substance against their conc. gradient. The energy comes from ATP

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98
Q

Where does the energy for active transport come from?

A

ATP

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99
Q

What is osmolarity a measure of?

A

Solute concentration

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100
Q

What does 1M of glucose have an osmolarity of?

A

1 osmole/L

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101
Q

What does 1M of NaCl have an osmolarity of?

A

2 osmole/L

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102
Q

What determines the cell volume?

A

Tonicity

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103
Q

If the ECT has a higher tonicity than the ICF what happens?

A

The solution is hypertonic

The cell will shrink as water leaves via osmosis to compensate

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104
Q

If the ECF has a lower tonicity than the ICF what happens?

A

The solution is hypotonic and the cell will swell as water enters the cell via osmosis to compensate

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105
Q

What is an isosmotic solution?

A

One in which there is an equal number of both penetrating and non-penetrating solutes on either side of the membrane

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106
Q

What is an isotonic solution?

A

One which there is an equal number of non-penetrating solutes on either side of the cell membrane

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107
Q

What happens in endocytosis?

A

When there is an invagination of the membrane to form a vesicle around the target substance to engulf it into the cell

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108
Q

What happens in exocytosis?

A

When a vesicle containing the substance is released from the cell

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109
Q

What is the function of epithelial tissue?

A

To cover surfaces and separate compartments

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110
Q

What do tight junctions do?

A

Seal intracellular space

Make waterproof

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111
Q

What do gap-junctions do?

A

Allow passage from cytoplasm to cytoplasm

Allowing cell to cell communication

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112
Q

What is a desosome?

A

An adhering junction
Cell to cell junction
That provides firm anchorage

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113
Q

What is a hemidesmosomes?

A

A cell to ECM junction

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114
Q

What does the function of epithelial tissue depend on the cell or ECF?

A

Cell

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115
Q

What function do cilia have?

A

Movement

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116
Q

What function do microvilli have?

A

Absorption

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117
Q

What cells are found in the liver?

A

Hepatocytes

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118
Q

Give an example of a function of hepatocytes?

A

Secretion

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119
Q

How are kidney cells arranged?

A

Into nephrons

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120
Q

Give some examples of functions of nephrons

A

Filtration of blood

Partial absorption of filtrate

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121
Q

Where do endocrine glands secrete to?

A

The blood

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122
Q

Where do exocrine glands secrete to?

A

The surface

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123
Q

Give an example of a exocrine gland

A

Sweat glands

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124
Q

What shape does a tubular glands have?

A

Tube

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125
Q

What shape does a acinar gland have?

A

Rounder

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126
Q

What is the consequence of abnormal over production of glandular function?

A

Pituitary giantism

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127
Q

What is the consequence of abnormal under production of glandular function?

A

Pituitary dwarfism

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128
Q

What percentage of body weight does collagen make up?

A

30%

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129
Q

How much can elastic fibres stretch?

A

1.5 times their length

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130
Q

Why is the skin an organ?

A

Because it contains all 4 types of tissue

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131
Q

What is the largest organ in the body?

A

The skin

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132
Q

What 3 layers is the skin composed of?

A

Epidermis
Dermis
Hypodermis

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133
Q

What is the epidermis composed of (tissue wise)?

A

Epithelium

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134
Q

What is the dermis composed of?

A

Connective tissue

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135
Q

What is the hypodermis composed of?

A

Fat

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136
Q

What is the function of the epidermis?

A

To form the boundary between internal and external environments

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137
Q

What is the function of the dermis?

A

To give structural strength

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138
Q

How many layers are there in the epidermis?

A

5

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139
Q

What are the 4 layers of the epidermis?

A

Stratum germinativum
Stratum Spinosum
Stratum granulosum
Stratum Corneum

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140
Q

What is the stratum germinativum bound to the basement membrane by?

A

hemidesmosomes

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141
Q

What is the stratum germinativum bound to other cells by?

A

Desosome

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142
Q

What is the stratum granuosum defined by the presence of?

A

Keratohyalin granules

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143
Q

Which layer of the epidermis is hard to identify?

A

Stratum corneum

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144
Q

Does the stratum corneum have cell organelles?

A

No

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145
Q

Does the stratum germinativum have cell organelles?

A

Yes - regular assortment of cell organelles

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146
Q

What 2 layers is the dermis composed of?

A

Papillary layer

Reticular layer

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147
Q

What type of connective tissue is the papillary layer composed of?

A

Loose connective tissue

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148
Q

What type of connective tissue if the reticular layer composed of?

A

Dense irregular connective tissue

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149
Q

Where is the stretch reflex found?

A

In all muscles

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150
Q

What is the simplest reflex?

A

Stretch reflex

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151
Q

What is an example of a stretch reflex?

A

The knee jerk reflex

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152
Q

What is the stretch reflex elicited by?

A

A sharp tap to the tendon

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153
Q

Why do tendons not contract?

A

Because they are inelastic

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154
Q

Where is the force from a sharp tap to the tendon transferred to?

A

Muscle fibres

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155
Q

What are the functions of bones in the body?

A

Mechanical
Protective
Metabolic
Haematopoies

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156
Q

What do bones provide support and attachment for?

A

Muscles
Tendones
Ligaments
Joints

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157
Q

What do bones protect?

A

Internal organs

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158
Q

What metabolic functions do bones have?

A

Mineral reservoir for calcium and phosphate homeostasis

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159
Q

In endochondral ossification where do bones form?

A

As cartilage

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160
Q

In intramembranous ossification what do bones form as?

A

A fibrous plate

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161
Q

Is there a cartilaginous phase in intramembranous ossification?

A

No

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162
Q

What invade the cartilage framework in Endochondral ossification?

A

Blood vessels

Osteogenic cells

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163
Q

What % of bone is composed of water?

A

20%

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164
Q

What % of bone is protein?

A

35%

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165
Q

What are the epiphyses of long bones composed of?

A

Trabecular (spongy) bone

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166
Q

How is cortical (hard) bone arranged?

A

In haversian systems

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167
Q

What gives bone it strength?

A

The collagen molecules form fibrils, which then form fibres and finally sheets

168
Q

What are osteoclasts responsible for?

A

For resorbing cells

169
Q

What are osteoblasts responsible for?

A

For laying down more bone

170
Q

Why are bones constantly remodelled?

A

To keep them at peak strength

171
Q

What are osteocytes derived from?

A

The differentiation of osteoblasts

172
Q

What do osteocytes act as?

A

Sensors of mechanical pressure and damage

173
Q

What are the 4 basic categories of amino acids?

A

Acidic
Basic
Uncharged polar
Non-polar

174
Q

Give examples of functions of proteins

A
Movement 
Protection 
Transport 
Enzymes 
Receptors 
Structural 
Storage
Hormones 
Control of gene expression
175
Q

What is the primary structure of a protein?

A

The sequence of amino acids in a polypeptide chain

176
Q

What is the secondary structure of a protein?

A

The spatial arrangement of amino acid residues - involves H bonding of the backbone

177
Q

What are the 2 arrangements in secondary structure?

A

Alpha helices

Beta pleated sheets

178
Q

What is the tertiary structure of a protein?

A

The interactions between the R groups of amino acids

179
Q

What interactions can occur between the R groups in amino acids?

A
Van der Waals 
Ionic Interactions 
Hydrogen bonding 
Disulphide bridges
Hydrophobic structures
180
Q

What is the quaternary structure of a protein?

A

When there is the interaction of more than one protein subunit

181
Q

What is a co-factor?

A

A non-protein component needed for activity

182
Q

What is a co-enzyme?

A

A complex organic molecule usually formed from vitamins

183
Q

What is a prosthetic group?

A

A cofactor covalently bound to the enzyme or very tightly associated with the enzyme

184
Q

What is an apoenzyme?

A

The protein component of an enzyme containing the prosthetic group

185
Q

What do enzymes increase?

A

The rate of a spontaneous reaction

186
Q

What do enzymes lower?

A

The activation energy of biochemical reactions

187
Q

What do enzymes accelerate the movement towards (but not change the position of)?

A

Equilibrium

188
Q

What does a large Km tell us about the affinity of the ES complex?

A

A less stable ES complex

The S has a low affinity for the active site

189
Q

What does a low Km tell us about the affinity of the ES complex?

A

That there is a more stable ES complex

The S has a high affinity for the active site

190
Q

What does the Km value tell us?

A

The affinity of the substrate for the active site

191
Q

Where do competitive inhibitors?

A

The active site

192
Q

How do competitive inhibitors bind?

A

Non-covalently

193
Q

Where do non-competitive inhibitors bind?

A

To a site other than the active site of the enzyme

194
Q

How do competitive inhibitors affect the Km?

A

Increase the Km as the affinity for the proper substrate decreases

195
Q

How is competitive inhibition overcome?

A

By increasing the substrate concentration

196
Q

Can non-competitive inhibition be overcome?

A

No

197
Q

What happens to Vmax in non-competitive inhibition?

A

The inhibitor cannot be displaced by increasing the conc. of the substrate so Vmax will decrease

198
Q

What can metabolites binding to allosteric enzymes act as?

A

Inhibitors or activators

199
Q

What is the concerted model of allosteric enzymes?

A

Each subunit exists in 2 different conformation
One is open (low Km)
One is closed (high Km)
With no substrate the enzyme flips between comformation
When 1 substrate binds it holds the enzyme in the open conformation

200
Q

What is the sequential model of allosteric enzymes?

A

There is no flipping
The binding to one subunit causes a conformation change to the next
And so on…

201
Q

What are the 3 major monosaccharides?

A

Glucose
Galactose
Fructose

202
Q

What are the 3 major disaccharides?

A

Maltose
Sucrose
Lactose

203
Q

Where is glucokinase found?

A

In the liver

204
Q

Where is hexokinase found?

A

In all the other tissues

205
Q

What are glucokinase and hexokinase to each other?

A

Isoenzymes

206
Q

What are isoenzymes?

A

Enzymes that catalyse the same reaction

207
Q

Are the Km and Vmax of hexokinase and glucokinase the same?

A

No they differ

208
Q

When will glucokinase pick up glucose?

A

When the glucose conc. is high

209
Q

Describe the Km and Vmax of hexokinase

A

Has a low Km

Low Vmas

210
Q

Why does hexokinase have a low Km?

A

So that glucose will bind even at low concentrations

211
Q

Why does hexokinase have a low Vmax?

A

As it means the tissues it is found in are quickly satisfied

212
Q

Why does glucokinase have a high Vmax?

A

So it can trap as much glucose as possible

213
Q

What is glycogen?

A

A polymer of glucose

214
Q

What enzyme synthesises glycogen?

A

Glycogen Synthase

215
Q

How is glycogen formed?

A

Glucogenin starts by binding to glucose from UDP-glucose to form chains of approx 8 subunits

216
Q

Between what alpha are the branches in glycogen?

A

a1-a6

217
Q

How often are the branches in glycogen?

A

Every 8 to 12 residues

218
Q

What is the net gain of ATP for every 1 molecule of glucose in glycolysis?

A

2 ATP

219
Q

What organelle dor RBC not have?

A

Mitochondria

220
Q

What are the 2 phases of glycolysis?

A

Investment stage

Pay off stage

221
Q

How many ATP are invested in the investment stage?

A

2ATP

222
Q

How many ATP are gained in the pay off phase?

A

4ATP

223
Q

What is the end product of glycolysis?

A

Pyruvate

224
Q

How many stages are there in glycolysis?

A

10

225
Q

What is the 1st stage of glycolysis?

A

Phosphorylation of glucose

226
Q

What is the 2nd stage in glycolysis?

A

The conversion of G-6-P to F-6-P

227
Q

What is the 3rd stage of glycolysis?

A

Phosphorylation of F-6-P to F-1, 6-bisP

228
Q

What is the 4th stage in glycolysis?

A

The cleavage of F-1,6biP

229
Q

What is the 5th stage of glycolysis?

A

The interconversion of triose sugars to give 2 of the same molecule

230
Q

What is the 6th stage in glycolysis?

A

Oxidation of G-3-P to 1,3-bisPG

231
Q

What is the 7th stage of glycolysis?

A

The P transfer from 1,3-bisPG to ADP

232
Q

What is the 8th stage in glycolysis?

A

The conversion of 3-PG to 2-PG

233
Q

What is the 9th stage in glycolysis?

A

Dehydration of 2-PG to PEP

234
Q

What is the 10th stage of glycolysis?

A

The transfer of P from PEP to ADP

235
Q

Why does NAD+ need to be regenerated?

A

Because it is needed for glycolysis q

236
Q

What doe NAD+ act as?

A

An electron acceptor

237
Q

What are the 3 fates of pyruvate?

A

Can enter the CAC to produce CO2 and water
Can be converted to lactate
Can be converted to ethanol (this occurs in yeast)

238
Q

What does the fate of pyruvate depend on?

A

The needs of the cell at any given time

239
Q

What is the main organism that converts pyruvate to ethanol?

A

Yeast and other micro-organisms

NOT IN HUMANS

240
Q

What is regenerated in converting pyruvate to ethanol?

A

NAD+

241
Q

When is pyruvate converted to lactate?

A

When the human cells are lacking O2

242
Q

How is pyruvate reduced to lactate?

A

Via fermentation

243
Q

What is regenerated in converting pyruvate to lactate?

A

NAD+

244
Q

How is NAD+ regenerated in the conversion of pyruvate to lactate?

A

The oxidation of NADH drives the recdution of pyruvate to lactate

245
Q

What do cells require for pyruvate to enter the CAC?

A

Oxygen

246
Q

What is pyruvate oxidised to form when entering the CAC?

A

Acetyl coenzyme A

247
Q

Where does the CAC occur?

A

Within the mitochondria

248
Q

What is bond between sugar monomers called?

A

Glycosidic bond

249
Q

Give example of tissues that rely entirely on glucose as their main energy source?

A

Brain
NS
RBC
Testes

250
Q

What is gluconeogenesis not a reverse of?

A

Glycolysis

251
Q

How many of the glycolysis reactions are reversible?

A

7 out of 10

252
Q

What prevents the reactions in glycolysis being reversible?

A

Large -ve

253
Q

How many reactions are there that can bypass the irreversible ones in glycolysis?

A

4

254
Q

How is pyruvate converted back to PEP?

A

Pyruvate - oxaloacetate - maltate - oxaloacetate- PEP

255
Q

How is lactate converted back to PEP?

A

Lactate- pyruvate - oxaloacetate - PEP

256
Q

What does reaction A of gluconeogenosis do?

A

Converts pyruvate to oxaloacetate

257
Q

What does reaction B of gluconeogenesis do?

A

Converts oxaloacetate to PEP

258
Q

What is converted to what in reaction C of gluconeogenesis?

A

F-1,6-BP to F-6-P

259
Q

What is happening in reaction C of gluconeogenesis?

A

Their is a dephosphorylation

260
Q

In reaction D of gluconeogenesis what is converted to what?

A

G-6-P is converted to glucose

261
Q

What is happening at reaction D of gluconeogenesis?

A

Their is a dephosphorylation

262
Q

Why is the conversion of F-6-P to G-6-P usually the end point for gluconeogenesis?

A

Because ending the pathway here allows the cells to ‘trap’ the glucose

263
Q

Which two sugars can enter glycolysis at various points?

A

Fructose and Galactose

264
Q

Where is most fructose metabolised?

A

In the liver

265
Q

What does the pentose phosphate pathway produce?

A

NADPH

266
Q

What are pentoses (5-C sugars) precursors for?

A

ATP, RNA and DNA

267
Q

What is NADPH used for in the liver?

A

Fatty acid synthesis

268
Q

What is NADPH used for in the mammary gland?

A

Fatty acid synthesis

269
Q

What is NADPH used for in the adrenal cortex?

A

Steroid synthesis

270
Q

What is NADPH used for in RBC?

A

As an antioxidant

271
Q

How many phases does the pentose phosphate pathway have?

A

2

272
Q

Is ATP consumed or produced in the pentose phosphate pathway?

A

No

273
Q

What does the 1st phase of the pentose phosphate pathway produce?

A

NADPH

274
Q

What does the 2nd phase of the pentose phosphate pathway do?

A

Interconverts G-6-P and pentose phosphate to form lots of different 3,4,5,6 and 7-C sugars

275
Q

What does NADPH link?

A

Catabolic and anabolic pathways

276
Q

What is NADP+ used as?

A

An electron carrier

277
Q

What does drinking lead to an increased what?

A

Blood lactate

278
Q

What does drinking lead to a decreased what?

A

Blood glc

279
Q

What does drinking inhibit?

A

Gluconeogenesis

280
Q

Why does drinking inhibit gluconeogenesis?

A

Because to breakdown the ethanol NAD+ is needed

But the liver needs all of this NAD+ for gluconeogenesis

281
Q

How does galactase join glycolysis?

A

Through conversion to glucose-1-phosphate by UDP

282
Q

What is the citric acid cycle also known as?

A

The krebs cycle

283
Q

Where does the CAC occur?

A

In the mitochondrial matrix

284
Q

What does the CAC pass onto?

A

The electron transport chain

285
Q

Does the CAC yield more or less energy than glycolysis?

A

More

286
Q

What is the CAC a gateway to?

A

Aerobic metabolism

287
Q

What is formed in the CAC?

A

NADH and FADH2

288
Q

What enters the CAC?

A

Acetyl CoA

289
Q

What are oxidised to produce acetyl CoA?

A

Pyruvate and FA

290
Q

What enzyme converts pyruvate to Acetyl CoA?

A

Pyruvate dehydrogenase

291
Q

Where is the only site of oxidative phosphorylation in eukaryotes?

A

Mitochondria

292
Q

What does the mitochondria utilise to produce ATP?

A

Proton gradients

293
Q

What are the folds in the mitochondria called?

A

Cristae

294
Q

Where is the majority of NADH and FADH2 produced?

A

In the mitochondrial matrix

295
Q

Where is a little NADH made?

A

In the cytoplasm

296
Q

Why is the glycerol phosphate shuttle necessary?

A

Because NADH is unable to cross the mitochondria membranes

297
Q

How does NADH eventually cross the mitochondrial matrix?

A

By passing its electrons onto FADH2

298
Q

What does complex 1 of the ETC work on?

A

NADH

299
Q

What happens at complex 1 of the ETC?

A

NADH is oxidised and its electrons are given to ubiquinone to give ubiquinol

300
Q

What does ubiquinol do at complex 1 of the ETC?

A

Pumps H+ ions into the inter membrane space

301
Q

What does the 2nd complex of the ETC work on?

A

FADH2

302
Q

What happens at complex 2 of the ETC?

A

Ubiquinone becomes ubiquonol

303
Q

What is another name for ubiquinone?

A

Q10

Co-enzymeQ10

304
Q

What happens at complex 3 of the ETC?

A

E- taken from ubiquinol and passed onto cytochrome C

305
Q

What does the cytochrome C do at complex 3 of the ETC?

A

Pumps protons into the intermembrane space

306
Q

What does complex 4 of the ETC do?

A

Takes the e- from cytochrome C and passes them to molecular O2

307
Q

Does complex 4 of the ETC pump protons across the intermmebrane space?

A

Yes

308
Q

What complexes of the ETC pump protons across the intermembrane space?

A

1,3,4

309
Q

What is overall created at the ETC by the pumping of electrons?

A

A proton gradient

310
Q

What eventually happens to the protons in the intermembrane space?

A

They eventually flow down their concentration gradient back into the matrix of the mitochondria

311
Q

How does H+ flow back down its conc. gradient?

A

By ATP synthase

312
Q

What reaction is the energy stored in the proton gradient used to convert?

A

ADP + Pi to ATP

313
Q

What is the final step in metabolising the food we eat?

A

The ETC

314
Q

Where doe ADP and Pi enter in ATP synthase?

A

The beta subunit

315
Q

What does the rotation of the Fo cyclinder cause?

A

Conformational change in the Beta subunits of F1

Causes to catalyse ADP to ATP

316
Q

What are the 3 conformational changes in the beta subunit of ATP synthase?

A

B subunit that binds ADP and Pi
B subunit that binds ATP
B subunit that doesn’t bind ATP

317
Q

What generates less ATP;NADH or FADH2

A

FADH2

318
Q

To which complex of the ETC does NADH feed into?

A

Complex 1

319
Q

To which complex of the ETC does FADH2 feed into?

A

Complex 2

320
Q

Ultimately what are food molecules broken down to?

A

CO2 and H2O

321
Q

What is the ETC coupled to?

A

ATP synthesis

322
Q

What is malignant hyperthermia caused by?

A

Cause by leaky mitochondrial membranes that uncouple the ETC and ATP synthase

323
Q

What is the thickness of the epidermis?

A

It varies around the body depending on its function

324
Q

What do melanocytes form?

A

Skin pigment

325
Q

What do merkel cells do?

A

Touch receptors

326
Q

What do keratinocytes contain?

A

Keratin

327
Q

What do keratinocytes extrude?

A

Lipids

328
Q

What do the arrector pili muscles do?

A

Attach to hair follicle root

The hair straightens when the muscle contracts

329
Q

What does the sebaceous gland secrete?

A

Sebum

330
Q

Where does sebaceous secrete to?

A

Into the hair follicle

331
Q

What is a good sign of overall health (a body part)?

A

The condition of nails

332
Q

What contributes to thermoregulation?

A

Sweat glands
Blood vessel dilation
Hair

333
Q

What is the repair tissue of skin?

A

Granulation tissue

334
Q

Why do we get scars?

A

Because after damage the skin is not as composed and nicely put together as it was originally

335
Q

Does one receptor always have one response?

A

No can have several responses

336
Q

What are the range of receptor types?

A

Receptors that are also ion channels
That are enzymes
That directly regulate enzymes
That work via G-proteins

337
Q

Does one cell have one type of receptor?

A

No it can have several receptors for different chemical signals

338
Q

Are receptors needed for lipophobic or lipophilic transmitters?

A

Lipophobic

339
Q

What is an ionotropic receptor?

A

Where the receptor is also an ion channel

340
Q

What is the intracellular domain of enzyme receptors?

A

Kinase domains

341
Q

What do kinase domains do?

A

Phosphorylate downstream cytoplasmic molecules

342
Q

When receptors are coupled directly to ion channels what responses are generated?

A

Slow EPSPs

Slow IPSPs

343
Q

What do receptors enable?

A

Specificity

344
Q

What is an agonist?

A

Something that mimics the normal effect of the receptor

345
Q

What is an antagonist?

A

Something that blocks the normal action of a receptor

346
Q

What is the relationship between agonist concentration and effect?

A

As conc. of agonist is increases more receptors are occupied and therefore effect increases

347
Q

What is the affinity for a drug?

A

The strength of chemical attraction between the drug and receptor

348
Q

What is the efficacy of an agonist?

A

How good the agonist is at activating that particular receptor

349
Q

Where are Ca2+ stores held?

A

Endoplasmic reticulum

350
Q

What ion is a really good messenger?

A

Ca2+

351
Q

What are some of the effects of Ca2+ as a messenger?

A

Directly affects target protein

I.e works on troponin

352
Q

What is the effect of G protein being coupled to adenyly cyclase?

A

Increases or decreases cAMP

Activates or inhibits PKA

353
Q

What is the effect of G protein being coupled to phospholipase C?

A

Produces diacylglycerol and inositol triphosphate

Activate PKC and releases Ca2+ from internal stores

354
Q

What is a drug?

A

Any chemical agent that affects a biological system

355
Q

What is the saturated response?

A

Maximum response

All receptors are saturated

356
Q

What does the size of drug response depend on?

A

Affinity

Efficacy

357
Q

Give an example of when antagonists are useful?

A

When they block pain receptors

358
Q

What do selective agonists do?

A

Enhance a good effect

359
Q

What do selective antagonists do?

A

Block a bad effect

360
Q

What does the AP in the axon open at the pre-synaptic terminal?

A

Ca2+ channels

361
Q

What does the opening of Ca2+ channels at the presynaptic terminal trigger?

A

The fusion of vesicles

Ach is released into the synaptic cleft

362
Q

Where does Ach go in the synaptic cleft?

A

Diffuses across and binds to the receptors on post synaptic

363
Q

What is the effect of Ach binding at the postsynaptic neuron (NMJ)?

A

Ligand gates Na+ and K+ channels are opened

364
Q

What is the end plate potential?

A

The potential at the NMJ

365
Q

What happens at the end plate potential?

A

It always reaches threshold so fires an AP

366
Q

What is excess Ach in the synaptic cleft removed by?

A

Actycholinesterase

367
Q

What is the first phase of the pentose phosphate pathway?

A

Oxidation of G-6-P to form lactone

NADPH is produced

368
Q

What is the 2nd phase of the pentose phosphate pathway?

A

The interconversion to form lots of different 3,4,5,6 and 7 sugars

369
Q

What is the golgi reflex the opposite of?

A

The stretch reflex

370
Q

What does the golgi tendon reflex prevent?

A

Muscles contracting so hard that the tendon is torn from the bone

371
Q

What is the golgi tendon reflex stiulated by?

A

Muscle contraction

372
Q

What happens in the golgi tendon reflex?

A

There is an inhibition of the agonist (contracting muscle)

There is an excitatory of the antagonist (relaxing muscle)

373
Q

Is the golgi tenodn reflex monosynaptic?

A

No

Polysynaptic

374
Q

Are flexor reflexes polysynaptic

A

Yes

375
Q

What can glutamate donate ammonia to?

A

Pyruvate to make alanine

376
Q

Is a peptide bond planar?

A

Yes

377
Q

What causes denaturation of proteins?

A

Heat, acids, solvents

378
Q

What does denaturation cause?

A

Loss of biological activity

379
Q

How is a prothetic group bonded?

A

Covalently

380
Q

What is the holoenzyme?

A

The whole enzyme

381
Q

What is specific for the active site?

A

The transition state

382
Q

Is E+S = ES reversible?

A

Yes

383
Q

What is the rte limiting step in enzymes?

A

Formation of product

384
Q

What is Vmax?

A

Maximum velocity

385
Q

What are ribozymes?

A

Enzymes made of RNA

386
Q

What do enzymes in the wrong place generally indicate?

A

Disease

387
Q

What is the combinations of CK?

A

BB
MM
BM

388
Q

What is CK2 isoform a diagnostic marker for?

A

Myocardial infarction

389
Q

What is random binding (enzymes)?

A

When the binding and release is random

390
Q

What is sequential binding?

A

When the binding and release has to be in a specific order

391
Q

What normally builds up and blocks in feedback inhibition?

A

End product

Blocks an enzyme in the pathway

392
Q

What does GAG form (muco)?

A

Mucous

Synovial fluid

393
Q

How is glucose absorbed in the villi?

A

Facilitated diffusion

Moves down with Na+ conc

394
Q

What does glucose absorption indirectly require?

A

ATP to pump Na+ back out

Maintaining Na+ gradient

395
Q

How is fructose absorbed?

A

GLUT 5

396
Q

Why is Glc changed to G-6-P?

A

So cells can trap it

397
Q

How is G-6-P trapped?

A

GLUT channels don’t recognise it

398
Q

Is glycogen osmotically active?

A

No

Osmotically inactive

399
Q

Do eosinophils contain granules?

A

Yes

400
Q

On first exposure to an allergen what happens?

A

Makes lot of IgE antibodies

Receptors bind to mast cells

401
Q

What is the most abundant complement protein?

A

C3

402
Q

Are NK cells in innate or adaptive immunity?

A

Both

It is in both camps

403
Q

What makes up the basement membrane?

A

Basal Lamina

Reticular Lamina

404
Q

What are 2 examples of secondary functions of epithelium?

A

Movement

Absorption

405
Q

Is simple epithelium one cell type?

A

No one layer but not one cell type

406
Q

What is myoepithelial?

A

Epithelium that turns into muscle

407
Q

What is an example of a steroid gland?

A

Adrenal cortex

408
Q

What is the cell that forms collagen?

A

Fibroblasts

409
Q

Why is glutamine transported in the blood not glutamate?

A

Because glutamine has no charge

And glutamate has a negative charge

410
Q

What do desosomes link?

A

Keratin

411
Q

What do adheren junction link?

A

Actin

412
Q

Why is carbon so central in the human body?

A

Because of its versatility

413
Q

What is the effect of a C=C bond?

A

Fixed arrangement

414
Q

Can C-C rotate freely?

A

Yes

415
Q

Where does digestion of Carbs start?

A

In the mouth

416
Q

Does the stomach have any carb digestion?

A

No