Brainscape's Knowledge GenomeTM

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


See full index

Advanced Human Physiology > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

Functions of neurons and nervous tissue

A

Initiate, integrate, conduct electrical signals

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

What is the most common connective tissue

A

loose connective tissue

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

What tissue makes up bones, tendons, and ligaments?

A

dense connective tissue

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

What are the functions of extracellular matrix

A

Scaffold for cellular attachments
Cell signaling
Collagen fibers/Elastin fibers

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

Homeostasis

A

fluctuation of processes within a predictable and often narrow range

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

Dynamic constancy

A

variation over a short period of time, but stable over a long period of time

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

Steady state

A

a variable is not changing, but energy is required to maintain constancy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Equilibrium

A

a variable is not changing, but no energy is required to maintain constancy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Set point

A

the “value” of the variable at steady state or equilibrium

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What would the effect on a pathway be if negative feedback was removed?

A

Too much (an overload) of the product would be produced

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

Feedforward

A

changes in regulated variables are anticipated and compensated for before the change actually occurs

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

Give an example of feedforward inhibition.

A

body temperature regulation

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

What are the components of homeostatic control mechanisms in reflexes? (figure 1.8 & 1.9)

A 
Stimulus
Receptor
Afferent pathway
Integrating center
Efferent pathway
Effector
Response
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Hormone-secreting gland cell pathway

A

Produces hormones that flow through blood vessels and targets cells in one or more distant places in the body

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

Neuron pathway

A

Produces an electrical signal that goes through a neurotransmitter to a neuron or effector in close proximity to site of neurotransmitter release

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

A local cell that produces a paracrine substance

A

targets cells in close proximity to site of neurotransmitter release

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

A local cell that produces an autocrine substance

A

autocrine substance acts on the same cell that secreted the substance

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

Can a neuron, endocrine gland cell, and other cell type release the same chemical messenger?

A

yes

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

Can a certain messenger have multiple functions?

A

yes; a particular messenger may function as a neurotransmitter, a hormone, or a paracrine or autocrine substance

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

Gap junctions

A

physical linkages connecting the cytosol between two cells, which allow molecules to move from one cell to an adjacent cell without entering the extracellular fluid.

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

juxtacrine signaling

A

the chemical messenger not actually being released from the cell producing it, but rather is located in the plasma membrane of that cell. When the cell encounters another cell type capable of responding to the message, the two cells link up via the membrane-bound messenger.

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

Adaptation

A

a characteristic that favors survival in specific environments.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Acclimatization

A

improved functioning of an existing homeostatic system; sometimes due to prolonged exposure to an environmental change

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

What is the most common process related to homeostasis?

A

circadian rhythm

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

Circadian rhythm

A

Cycles approximately once every 24 hours. Waking and sleeping, body temperature, hormone concentrations in the blood, the excretion of ions into the urine, and many other functions undergo circadian variation.

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

What atoms make up 99.3% of total atoms in the body?

A

hydrogen, oxygen, carbon, and nitrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

atomic number

A

number of protons in an element

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

atomic mass

A

The atomic mass scale indicates an atom’s mass relative to the mass of other atoms.

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

gram atomic mass

A

amount of the element, in grams, equal to the numerical value of its atomic mass

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

How many atoms does one gram of atomic mass contain?

A

6×10^23 atoms - Avogadro’s number

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

electrolytes

A

ionic forms of mineral elements

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

electronegativity

A

The measure of an atom’s ability to attract electrons in a covalent bond

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

Polar covalent bonds

A

electrons are shared un-equally

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

Non-polar covalent bonds

A

electrons are shared equally

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

Molecules with polar covalent bonds are…

A

soluble in water

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

Molecules with non-polar covalent bonds are…

A

insoluble in water

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

ionic bond

A

The strong attraction between two oppositely charged ions

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

Hydrogen bonds

A
  • occur when two polar molecules are in close proximity.
  • attraction between hydrogen atom of one molecule and oxygen or nitrogen atom of another molecule
  • very weak—4% strength of polar covalent bond
  • in large number, hydrogen bond have implications pertaining to molecular structure
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Two commonly encountered groups of atoms that undergo ionization in molecules are the…

A

carboxyl group (—COOH) and the amino group (“—” NH_2 )

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

Free radicals

A
  • contain a single (unpaired) electron in an orbital of their outer shell
  • are unstable and highly reactive
  • may remove an electron from another atom to fill their outer shell
  • the atom that lost its electron becomes another free radical
  • formed by the actions of certain enzymes in some cells, such as types of white blood cells that destroy pathogens
  • can be produced in the body following exposure to radiation or toxin ingestion.
  • can do considerable harm to the cells of the body.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Examples of biologically important free radicals

A
  • superoxide anion, O_2∙–
  • hydroxyl radical, OH∙
  • nitric oxide, NO∙
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

How much of total body weight is made up of water?

A

60%

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

Hydrolysis

A

involves the breaking of a chemical bond with the additions of elements of water (“—” H and “—” OH) to the products formed

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

How does water move in osmosis?

A

low to high concentrations

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

hydrophilic

A

“water loving”

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

hydrophobic

A

“water fearing”

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

Amphipathic molecules

A

a special class of molecules that have a polar or ionized region at one site and a nonpolar region at another site.

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

Solute concentration

A

the amount of solute present in a unit volume of solution.

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

Formula for molarity:

A

M=mol/liter

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

Acid

A

releases protons (hydrogen ions) in solution

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

Base

A

accepts protons (hydrogen ions) in solution

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

formula for pH

A

pH = -log[H+}

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

What is the homeostatic range for pH in the extracellular fluid in the body?

A

7.35-7.45

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

Carbohydrates

A

Disaccharides and Polysaccharides

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

What are the subunits of carbohydrates

A

Monosaccharides

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

Subclasses of lipids

A

Triglycerides
Phospholipids
Steroids
Fatty acids

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

Subunits of triglycerides

A

Fatty Acids, Glycerol

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

Subunits of phospholipids

A

Fatty Acids, Glycerol, Phosphate

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

Proteins

A

Polypeptides

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

Subunits of proteins

A

amino acids

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

Nucleic acids

A

DNA & RNA

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

Subunits of nucleic acids

A

nucleotides

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

What organic molecule makes up the largest percentage of body weight?

A

proteins (17%)

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

Glycogen

A

exists in the body as a reservoir of available energy that is stored in the chemical bonds within individual glucose monomers.

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

Hydrolysis of glycogen

A

leads to the release of the glucose monomers into the blood, thereby preventing blood glucose from decreasing to dangerously low levels.

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

Glucose

A

often called “blood sugar” because it is the major monosaccharide found in the blood.

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

What atoms are lipids prominently composed of?

A

hydrogen and carbon atoms

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

What is the physiological importance of lipids

A

energy source, cell membranes, cell signaling

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

Fatty acid

A

chain of carbon and hydrogen atoms with an acidic carboxyl group at one end.

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

saturated fatty acid

A

carbons are linked by single covalent bonds

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

unsaturated fatty acid

A

contain one or more double bonds between carbon atoms

72
Q

monounsaturated

A

one double bond is present

73
Q

polyunsaturated

A

more than one double bond present

74
Q

Triglycerides

A

glycerol (a three-carbon sugar-alcohol) bonds to three fatty acids

75
Q

What constitutes for the majority of the lipids in the body

A

triglycerides

76
Q

Where are triglycerides synthesized

A

the liver

77
Q

Where are triglycerides stored and what is their function?

A

adipose tissue where they serve as an energy reserve

78
Q

Phospholipids

A

glycerol bound to two fatty acids and a phosphate.

79
Q

Phosphate

A

polar, hydrophilic region

80
Q

Fatty acid

A

non-polar, hydrophobic region

81
Q

Are phospholipids hydrophylic or hydrophobic?

A

BOTH! They are amphipathic

82
Q

What does the amphipathic structure of phospholipids allow them to form?

A

Lipid bilayers of cellular membranes

83
Q

Steroids

A

structure: Four interconnected rings of carbon atoms form the skeleton of every steroid.
NOT WATER SOLUBLE

84
Q

Examples of steroids

A
  • cholesterol cortisol from the adrenal glands

- female (estrogen) and male (testosterone) sex hormones secreted by the gonads.

85
Q

Proteins account for about how much of the organic material in the body?

A

50%

86
Q

What are proteins composed of

A

carbon, hydrogen, oxygen, nitrogen, and small amounts of other elements, notably sulfur

87
Q

Structure of amino acids

A
  • terminal carbon atom
  • amino (“—” NH_2 )
  • carboxyl (—COOH)
  • hydrogen atom
  • amino acid side chain or R-group (amino acid side chain)
88
Q

How are essential amino acids obtained?

A

diet

89
Q

Primary structure of proteins

A

the number of amino acids in the chain, and the specific sequence of different amino acids.

90
Q

What is a polypeptide?

A

analogous to a linear string of beads, each bead representing one amino acid.

91
Q

Secondary structure of proteins due to hydrogen bonds

A
  • alpha helix (coil)

- beta pleated sheet

92
Q

What role do beta pleated sheets and alpha helices play in proteins?

A

they tend to impart upon a protein the ability to anchor itself into a lipid bilayer.

93
Q

Tertiary structure of proteins due to side chains

A
  • Folding

- Functional protein

94
Q

What are the 5 main structures that determine tertiary structure of proteins?

A
  • hydrogen bonds between side groups of amino acids or with surrounding water molecules;
  • ionic interactions between ionized regions along the chain;
  • interactions between nonpolar (hydrophobic) regions;
  • covalent disulfide bonds linking the sulfur-containing side chains of two cysteine amino acids; and
  • van der Waals forces.
95
Q

Quaternary structure of proteins

A

polymerization of tertiary structures

ex- hemoglobin

96
Q

Nucleic acid functions

A

storage, expression, and transmission of genetic information.

97
Q

Nucleotides

A

monomeric subunits of nucleic acids, which contain a phosphate group, a five-carbon sugar, and a nitrogenous base

98
Q

Purine bases:

A
  • adenine (A) and guanine (G)

- double ring

99
Q

Pyrimidine bases

A
  • cytosine (C) and thymine (T)

- single ring

100
Q

What does the adenine base pair with

A

thymine

101
Q

What base does guanine pair with

A

cytosine

102
Q

Deoxyribonucleic Acid (DNA)

A

Double helix and hydrogen bonds between the bases

103
Q

How does Ribonucleic Acid (RNA) differ from DNA

A
  • Single chain of nucleotides
  • Sugar in each nucleotide is ribose rather than deoxyribose
  • Pyrimidine base thymine in DNA is replaced by the pyrimidine base uracil (U).
    • Uracil pairs with adenine
104
Q

Cytoplasm

A

everything outside of the nucleus

105
Q

Cytosol

A

fluid component of the cytoplasm

106
Q

ICF (intracellular fluid)

A

Cytosol + Fluid in the nucleus

107
Q

Functions of Plasma Membranes

A
  • Regulate the passage of substances into and out of cells and between cell organelles and cytosol.
  • Detect chemical messengers arriving at the cell surface.
  • Link adjacent cells together by membrane junctions.
  • Anchor cells to the extracellular matrix
108
Q

Membrane

A

double layer of lipid molecules containing embedded proteins.

109
Q

Major membrane lipids

A

Phospholipids and cholesterol

110
Q

What is the function of the cholesterol in the plsama membrane

A

Cholesterol have a coordinated functionin maintaining an intermediatefluidity of the plasma membrane. This contrasts with intracellular membranes whichcontain very little cholesterol.

111
Q

Integral membrane proteins

A
  • closely associated with the membrane lipids
  • cannot be extracted from the membrane without disrupting the lipid bilayer
  • amphipathic
  • most integral proteins span the entire membrane and are referred to as transmembrane proteins.
112
Q

Functions of transmembrane proteins

A
  • form channels through which ions or water can cross the membrane,
  • whereas others are associated with the transmission of chemical signals across the membrane
  • the anchoring of extracellular and intracellular protein filaments to the plasma membrane.
113
Q

Peripheral membrane proteins

A
  • are not amphipathic
  • do not associatewith the nonpolar regions of the lipids in the interior of the membrane.
  • located at the membrane surface where they are bound to the polarregions of the integral membrane proteins.
114
Q

Types of membrane junctions

A
  • desmosomes
  • tight junctions
  • gap junctions
115
Q

Integrins

A

transmembrane proteins that bind to specific proteins in the extracellular matrix and link them to membrane proteins on adjacent cells.

116
Q

Desmosomes

A

hold cells together but allow for stretching (skin)

117
Q

Cadherins

A

proteins that extend from the cell into the extracellular space, where they link up and bind with cadherins from an adjacent cell.

118
Q

How are desmosomes characterized?

A

They are characterized by accumulations of protein known as “dense plaques” along the cytoplasmic surface of the plasma membrane.

119
Q

Tight junctions

A

form a barrier (epithelium of gut or bladder)

120
Q

Where are desmosomes limited to?

A

disk-shaped are of the membrane

121
Q

Where does the tight junction occur?

A

the tight junction occurs in a band around the entire circumference of the cell

122
Q

Gap Junctions

A

form protein channels linking the cytosols of two adjacent cells (myocardium, transmission of electrical activity)

123
Q

Can proteins pass through channels in gap junctions?

A

No, gap junctions are channels for small molecules such as ions

124
Q

What process turns DNA into RNA?

A

Transcription

125
Q

What process turns RNA into PROTEIN

A

Translation

126
Q

How many different ways can the four bases of DNA be arranged?

A

64

127
Q

What triplets are stop signals?

A
  • UAA
  • UAG
  • UGA
128
Q

What happens in transcription?

A
  • RNA polymerase binds to the promoter region of a gene and separates the two strands of the DNA double helix in the region of the gene to be transcribed.
  • Free ribonucleotide triphosphates base-pair with the deoxynucleotides in the template strand of DNA.
  • The ribonucleotides paired with this strand of DNA are linked by RNA polymerase to form a primary RNA transcript containing a sequence of bases complementary to the template strand of the DNA base sequence.
  • RNA splicing removes the intron-derived regions, which contain noncoding sequences, in the primary RNA transcript and splices together the exon-derived regions, which code for specific amino acids, producing a molecule of mature mRNA.
129
Q

Translation

A
  • The mRNA passes from the nucleus to the cytoplasm, where one end of the mRNA binds to the small subunit of a ribosome.
  • Free amino acids are linked to their corresponding tRNAs by aminoacyl-tRNA synthetase.
  • The three-base anticodon in an amino acid–tRNA complex pairs with its corresponding codon in the region of the mRNA bound to the ribosome.
  • The amino acid on the tRNA is linked by a peptide bond to the end of the growing polypeptide chain.
  • The tRNA that has been freed of its amino acid is released from the ribosome.
  • The ribosome moves one codon step along mRNA.
  • The previous four steps are repeated until a termination sequence is reached, and the completed protein is released from the ribosome.
  • In some cases, the protein undergoes posttranslational processing in which various chemical groups are attached to specific side chains and/or the protein is split into several smaller peptide chains.
130
Q

Mutations

A
  • Chemicals or ionizing radiation can cause structural changes to DNA resulting in a change in the nucleotide sequence.
  • A change in nucleotide sequence may lead to a change in the structure of a protein.
  • Changes in protein structure may impair cell function or may cause cell death.
131
Q

Protein Degradation

A
  • Different proteins degrade at different rates.
  • A denatured (unfolded) protein is more readily degraded than a protein with an intact conformation.
  • Proteins can be targeted for degradation by the attachment of a small peptide, ubiquitin, to the protein. This peptide directs the protein to a protein complex known as a proteasome, which unfolds the protein and breaks it down into small peptides.
132
Q

Ligand

A
  • molecule (including another protein) or ion that binds to a protein by one of the following forces:
  • electrical attractions between oppositely charged ionic or polarized groups on the ligand and the protein, or
  • weaker attractions due to hydrophobic forces between nonpolar regions on the two molecules.
133
Q

Binding Site

A

region of a protein to which a ligand binds

134
Q

How many binding sites can a protein have?

A

It can have multiple

135
Q

What does the binding of the ligand do to the protein?

A

It either activates the protein or inhibits the protein

136
Q

Chemical specificity

A

ability of a protein-binding site to bind specific ligands

137
Q

What does specificity depend on?

A

conformation

138
Q

Affinity

A

strength of ligand-protein binding

139
Q

What does the affinity of a binding site determine?

A

how likely it is that a bound ligand will leave the protein surface and return to its unbound state.

140
Q

What is the strength of a bond with high affinity?

A

strong

141
Q

What is the strength of a bond with low affinity?

A

weak bond

142
Q

What happens when a protein has a high-affinity binding site for a ligand?

A

very little of the ligand is required to bind to the protein

143
Q

Saturation

A

the fraction of total binding sites that are occupied at any given time.

144
Q

The percent saturation of a binding site depends upon what two factors?

A

1) the concentration of unbound ligand in the solution

2) the affinity of the binding site for the ligand

145
Q

Allosteric modulation

A

an allosteric protein has two binding sites

146
Q

Functional site (aka active site)

A

carries out the protein’s physiological function

147
Q

Regulatory site

A

a modulator molecule binds to the regulatory site and changes the conformation of the functional site

148
Q

Covalent modulation

A

covalent bonding of charged chemical groups to some of the protein’s side chains.

149
Q

Phosphorylation

A

covalent modulation by adding a phosphate group (negatively charged)

150
Q

Protein kinase

A

enzyme that mediates phosphorylation

151
Q

Phosphoprotein phosphatase

A

enzyme that mediates de-phosphorylation

152
Q

Catabolism

A

the breakdown of organic molecules

153
Q

Anabolism

A

the synthesis of organic molecules

154
Q

What do chemical reactions do?

A

break and form chemical bonds.

155
Q

How is breakdown and synthesis of organic molecules achieved?

A

through chemical reactions

156
Q

Determinants of reaction rates:

A

Reactant concentration
Activation energy
Temperature
Catalyst

157
Q

What does a greater concentration do to a reaction rate:

A

the reaction rate incerases

158
Q

what does a greater activation energy do for reaction rate?

A

slower reaction rate

159
Q

what does a higher temperature do for reaction rate?

A

increases reaction rate

160
Q

what does the presence of a catalyst do fro a reaction rate?

A

it increases reaction rate

161
Q

Reversible Reactions

A
  • A+B⇌C+D+Small amount of energy

- At chemical equilibrium, product concentrations are only slightly higher than reactant concentrations.

162
Q

Irreversible Reactions

A
  • E+F⇌G+H+Large amount of enery

- At chemical equilibrium, almost all reactant molecules have been converted to product.

163
Q

Law of Mass Action

A

The direction of a chemical reaction is determined (in part) by the concentrations of reactants and products.

164
Q

Enzymes

A

protein molecules, so an enzyme can be defined as a protein catalyst.

165
Q

What do enzymes do to activation energy? What do they do to biological reactions?

A

Enzymes lower the activation energy and make biological reactions proceed at a faster reaction rate.

166
Q

cofactors

A

Cofactors bind to an enzyme and alter the enzyme’s conformation to facilitate its interaction with a substrate.

167
Q

Enzyme-mediated reactions are regulated by what three major factors?

A
  • substrate concentration
  • enzyme concentration
  • enzyme activity
168
Q

Metabolic Pathways

A
  • Multienzyme pathways are the basis of cellular metabolism.

- An example is the transfer of energy released from the breakdown of fuel molecules to ATP.

169
Q

Essential Nutrients:

A

water, minerals, amino acids, fatty acids

170
Q

Essential mineral elements

A
  • 7 major mineral elements

- 13 trace elements

170
Q

Essential mineral elements

A
  • 7 major mineral elements

- 13 trace elements

171
Q

Essential amino acids

A 
Histidine
     Isoleucine
     Leucine
     Lysine
     Methionine
     Phenylalanine
     Threonine
     Tryptophan
     Valine
172
Q

Essential fatty acids

A

Linoleic acid

Linolenic acid

173
Q

Other essential nutrients

A

Inositol
Choline
Carnitine

174
Q

Water-soluble vitamins

A 
B1: thiamine
B2: riboflavin
B6: phridoxine
B12: cobalamine
Niacin Pantothenic acid
Folic acid
Biotin
Lipoic acid
Vitamin C
175
Q

Fat-soluble vitamins

A

Vitamin A
Vitamin D
Vitamin E
Vitamin K

Advanced Human Physiology (2 decks)

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