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Animal Physiology > quiz 8 > Flashcards

quiz 8 Flashcards

1
Q

how did we measure solute concentration

A

measured freezing point depression using an osmometer

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2
Q

the more solute the ___ freezign point depression

A

greater

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3
Q

what is the freezing point of salt water

A

-1.86

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4
Q

what is an osmole

A

1000mmoles/L

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5
Q

how does an osmometer measure freezing point depression

A

measured kinetic energy given off from supercooling of sample

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6
Q

invertebrate plasma is mostly what

A

water (not much formed elements)

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7
Q

what kind of invertebrates have a higher concentration of ions in their plasma

A

insects have higher ion concentrations

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8
Q

what are the elements besides formed elements in insect blood

A

inrganic ions, organic ions, proteins

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9
Q

what is an example of an ion invertebrates have a lot of

A

inverts have 10-15x more K than verts (40-50mM)

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10
Q

insects have more ______ ____ in relation to vertebrates

A

inorganic ions

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11
Q

herbivore insects have lower ____ ratios

A

Na/K

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12
Q

what are the most abundant organic ions in insects

A

treehalose and proline

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13
Q

what is trehalose

A

disaccharide of glucose (replaces glucose)

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14
Q

what is proline used for in insects

A

lepidopterans use proline for their metabolism

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15
Q

instead of antibodies in the blood, what do insects use

A

phagocytic cells

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16
Q

what blood component that isnt a formed element is most analogous to human blood

A

the proteins in the plasma

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17
Q

how much dissolved oxygen is in plasma

A

0.3mL/100mL

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18
Q

how much oxygen is in the Hb of blood

A

20mL/100mL

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19
Q

respiratory pigments are also called

A

respiratory proteins

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20
Q

pigments do

A

evoke a colour change

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21
Q

what kind of mer are respiratory pigments

A

oligomers

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22
Q

respiratory pigments are often conjugated with what

A

a metal ion

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23
Q

what are the 4 respiratory pigments

A

hemoglobin, hemocyanin, chlorocruorin, hemerythrin

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24
Q

what is the function of a respiratory pigment

A

reversible binding of oxygen and carbon dioxide

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25
Q

why is it vital to have respiratory pigments

A

aid in bufferring the pH of blood

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26
Q

when does a change in respirator pigment colour happen

A

when oxygen is bound or not bound

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27
Q

what is the most abundant resp. pigment in inverts

A

hemocyanin

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28
Q

what phenomena are resp. pigments

A

enzyme substrate complex

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29
Q

what is the most widespread resp. pigment

A

hemoglobin

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30
Q

what is the only resp. pigment in verts

A

hemoglobin

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31
Q

what mer is hemoglobin

A

oligomer in most

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32
Q

when is hemoglobin not oligomer

A

agnathans have it as a monomer

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33
Q

how big is monomeric hb

A

18kD

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34
Q

how big is oligomeric hb

A

68kD

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35
Q

what mer is hemoglobin in verts

A

tetramer

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36
Q

what are the 4 components of vert hb

A

2 alpha chains, 2 beta chains

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37
Q

how many amino acids are there per hb chain

A

145 amino acids

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38
Q

what is the name for monomeric hemoglobin

A

myoglobin

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39
Q

where can myoglobin be found in humans

A

in muscle tissue of humans

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40
Q

what does iron do in the hb

A

holds on to o2 in high o2 conditions and releases o2 in low o2 conditions

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41
Q

what is the heme group on hb

A

porphyrin ring

42
Q

what part of hb has the iron

A

heme has the ferrous iron

43
Q

where is hb found

A

in rbc

44
Q

what is the size of hb intracellular

A

20-30kD

45
Q

what is the size of hb extracellular

A

2000-3000kD

46
Q

where is extracellular hb

A

in plasma freely floating

47
Q

what is the binding dynamic in hb

A

cooperativity

48
Q

what colour is hemocyanin when bound with o2

A

blue

49
Q

what is the difference between hb and hc

A

pretty much only difference is the conjugated metal

50
Q

what metal does hc use

A

copper

51
Q

what is the second most widespread resp. pigment

A

hemocyanin

52
Q

what animals have hc

A

crustaceans and mollusks (cephalopods and gastropods)

53
Q

what mer is hemocyanin

A

oligomer

54
Q

how is copper bound in hc

A

direct binding of copper to histidine residues in subunit

55
Q

is hc intra or extracellular

A

hc is always extracellular

56
Q

what are histidine residues analogous to in hb

A

hc histidine residues = hb porphyrin ring

57
Q

what are the two less common resp. pigments

A

hemerythrin and chlorocruorin

58
Q

what animals have hemerythrin

A

brachiopods, priapulids, sipunculids, 1 polychaete

59
Q

what size are hemerythrin

A

16-125kD trimer or octamer

60
Q

where can hemerythrin be found in the blood

A

intra or extracellullarly

61
Q

what are the metals in hemerythrin

A

2 ferric ions per subunit that is attached to histidine residues

62
Q

what other resp. pigment is most like hemoglobin

A

chlorocruorin

63
Q

what animals have chlorocruorin

A

polychaetes

64
Q

where in blood can chlorocruorin be can

A

extracellular

65
Q

what size is chlorocruorin

A

3000kD

66
Q

how many subunits does chlorocruorin have

A

can have several dozen sub units

67
Q

how is chlorocruorin like hb

A

uses ferric iron and porphyrin ring (its just too big to be hb)

68
Q

what are the coined terms for hb reversible binding

A

oxyhemoglobin vs deoxyhemoglobin

69
Q

what does reversible binding do in hb

A

changes levels of oxygen throughout the body

70
Q

whats weird about the loading affinity for o2 in hb

A

loading first o2 is hard, then loading affinity increases so its easier to bind more o2

71
Q

why is the o2 affinity in hb observed

A

due to subunit conformational changes

72
Q

what kind of pattern does cooperativity follow

A

sigmoidal

73
Q

what can modulate the binding dynamics in hb

A

ph, temp, organophosphates

74
Q

how does ph change binding dynamics

A

h ion reduces affinity which favours unloading of o2 from hb

75
Q

how can temp change binding dyanamics

A

high temp reduces affinity which favours unloading of o2 from hb

76
Q

how do organophosphates change binding dynamics

A

elevated 2,3 DPG reduces affinity which favours unloading of o2 from hb

77
Q

what is the saturation at alveolar gas exchange concentration

A

98%

78
Q

what is the bohr effect

A

there is a right shift at lower pH in blood to allow for the unloading of o2 in blood (affinity of Hb for O2)

79
Q

what is the point of being aerobic as long as possible

A

the longer youre aerobic, the less fatigue you will get in a time span

80
Q

what organism has the root effect

A

fish with swim bladders

81
Q

what are the two kind of gas bladders

A

physostomic and physoclistic

82
Q

what is physostomic swim bladder

A

gulping

83
Q

what is physoclistic swim bladder

A

dissolved gasses in blood go into gas vessel (Hb sensitive)

84
Q

what are two allosteric modulators

A

ATP and GTP

85
Q

what are three ways to transport carbon dioxide

A

respiratory pigments, dissolved in solution, bicarbonic-carbonic acid system

86
Q

how much of total co2 in body is carried by hb

A

about 10%

87
Q

how much total co2 is moved by dissolved in solution

A

5-7%

88
Q

how much total co2 is moved by bicarbonic-carbonic system

A

85%

89
Q

how do respiratory pigments remove co2

A

reversible binding to amino acid residues

90
Q

how does dissolved in solution remove co2

A

dissolves into plasma and some into RBC cytoplasm by pressure

91
Q

how does bicarbinc-carbinc acid system remove co2

A

with the use of carbonic anhydrase

92
Q

where is carbonic anhydrase found

A

in RBC and apical surface of endothelium in plasma

93
Q

describe the bicarbonic-carbonic acid system

A

co2 in RBC and carbonic anhydrase combine with water to make carbonic acid that is dissoiated into bicarbonate and hydrogen ions, hydrogen ions bind to proteins (like hb), then chloride exchange puts bicarbonate into plasma

94
Q

what are the three types of blood ph regulation

A

immediate regulation, intermediate term, long term

95
Q

how does immediate regulation of blood ph work

A

using blood buffers

96
Q

what are examples of blood buffers

A

bicarbonate, albumin, hemoglobin

97
Q

how do blood buffers work

A

reversible binding so ph can be stabilized at a set point

98
Q

how does intermediate term blood ph regulation work

A

elimination of co2 via gas exchange systems

99
Q

how does long term blood ph regulation work

A

excretory systems to remove hydrogen ions

100
Q

what is the standing titer of co2

A

5mmHg

Animal Physiology (9 decks)

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