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ANSC 315 > Module 5- Protein metabolism > Flashcards

Module 5- Protein metabolism Flashcards

1
Q

what is protein

A

organic compound in feed that contains N

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2
Q

T or F: animals require amino acids, not proteins

A

T

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3
Q

how many amino acids are there

A

20

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4
Q

T or F: skeletal muscle is a storage for amino acids

A

F

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5
Q

what % of protein is found in skeletal muscle vs body organs, skin & blood

A

40, 25

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6
Q

T or F: all enzymes in our body are proteins

A

T

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7
Q

hydrolases

A

cleave compounds

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8
Q

isomerases

A

transfer atoms in a molecule

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9
Q

ligases

A

join compounds

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10
Q

oxidoreductases

A

transfer electrons

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11
Q

transferases

A

move functional groups

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12
Q

hormones

A

produced in endocrine glands
- transported through bloodstream to target tissues

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13
Q

T or F: all hormones are proteins

A

F

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14
Q

what 3 hormones are made of proteins

A

1) insulin
2) growth hormone
3) glucagon

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15
Q

2 contractile proteins

A

actin & myosin

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16
Q

fibrous proteins

A

keratin & collagen

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17
Q

2 groups of functional proteins

A

1) transporters
2) nutrient transporters

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18
Q

ceruloplasmin

A

transport copper

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19
Q

nutrient transporters function

A

expressed in cell membrane, responsible for uptake of nutrients into the cell

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20
Q

transporters function

A

transports different metabolites in the body

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21
Q

Na-dependent amino acid transporter

A

responsible for uptake of Na & AA

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22
Q

T or F: proteins can act as buffers

A

T

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23
Q

how do proteins act as acid-base buffers?

A

1) low pH -> AA accept H ions to increase pH
2) high pH -> AA release H ions = decrease pH

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24
Q

how does too much protein impact fertility?

A

ammonia can make acidic uterine environment

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25
Q

4 parts to an AA structure

A

1) central C atom
2) carboxylic group
3) amino group
4) side chain/R group -> what differs

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26
Q

physiological pH

A

7

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27
Q

at physiological pH, what form is the carboxylic group in?

A

dissociated
COO- + H

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28
Q

conditionally essential AA + example

A

requirement based on physiological state
- glycine in poultry

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29
Q

T or F: cysteine can reduce amount of dietary methionine required

A

T

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30
Q

phenylketonuria

A

elevation of phenylalanine in blood

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31
Q

aliphatic amino acids

A

have aliphatic side chains (methyl groups)

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32
Q

what are the 2 sulfur containing amino acids

A

cystenine & methionine

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33
Q

dicarboxylic AA

A

have 2 carboxylic acid groups = negatively charged

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34
Q

bibasic AA

A

have 2 amino groups
postive net charge

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35
Q

neutral AA

A

1 carboxylic + 1 amino group

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36
Q

negatively charged AA have an additional ( ) group while positively charged AA have additional ( ) group

A

carboxylic, amino

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37
Q

what 2 forms do AA exist in

A

L & D

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38
Q

what forms of AA are more abundant

A

L

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39
Q

monosaccharide enzymes recognize what form of AA

A

D

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40
Q

T or F: D isomers can be converted to L isomers but not vice versa

A

T

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41
Q

T or F: no enzymes available to convert L to D form of lysine

A

T

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42
Q

peptide bond links ( ) AA together

A

2

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43
Q

polypeptides vs proteins

A

polypeptides: less then 20 AA
proteins: more than 20 AA

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44
Q

T or F: no 2 proteins will be the same

A

T

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45
Q

how do proteins differ?

A

their sequence of AA

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46
Q

what is the sequence of AA determined by?

A

genetically by DNA

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47
Q

T or F: polypeptide backbones do not differ in AA

A

T

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48
Q

T or F: misfolded proteins are not functional

A

T

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49
Q

proteins in the ( ) structure are harder to digest

A

beta sheet

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50
Q

secondary structure of proteins

A

electrostatic attractions cause it to fold within itself
- alpha helix
- b sheets

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51
Q

tertiary structure of proteins have a ( ) bond

A

disulfide

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52
Q

quaternary structure of proteins

A

2+ polypeptide chains are interacting with each other

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53
Q

lactosynthase

A

synthesizes lactose in mammary gland

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54
Q

example of protein with a quaternary structure

A

hemoglobin

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55
Q

what 2 things does a primary protein structure determine?

A

1) AA profile
2) quantities of AA available

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56
Q

T or F: feather meal is not digestible due to beta sheets

A

T

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57
Q

how can feed with low digestibility be altered to improve it?

A

hydroylze

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58
Q

T or F: barley is very digestible bc it contains very little beta sheets

A

T

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59
Q

tertiary & quaternary structure of a protein are more involved with ( ) rather than nutrition

A

protein functionality

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60
Q

exogenous

A

derived in diet

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61
Q

example of a plant vs animal derived exogenous protein source

A

plant: soybean, canola meal
animals: fish meal

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62
Q

3 things that will decrease ability of GI tract to reclaim endogenous proteins

A

1) high fiber
2) anti-nutritional factors
3) tannins

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63
Q

protease enzymes perform

A

hydrolysis

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64
Q

T or F: protein digestion takes place in the monogastric mouth

A

F

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65
Q

chemical digestion in monogastric stomach

A

HCI + pepsin

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66
Q

pepsin is the ( ) form of pepsinogen

A

active

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67
Q

what do chief cells produce

A

gastric lipase

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68
Q

what is pepsinogen activated by

A

HCI

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69
Q

HCI function in stomach

A

denatures proteins = larger surface area

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70
Q

monogastric stomach pH

A

1-2

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71
Q

why does the pancreas not secrete enzymes instead of proenzymes?

A

bc they will break don the pancreas

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72
Q

T or F: proenzymes are active

A

F

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73
Q

what does acidic chyme in the proximal duodenum stimulate?

A

pancreatic juice which contains secretin & CCK to neutralize the chyme

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74
Q

endopeptidases vs exopeptidases

A

endo: digest polypeptide chain from the middle
exo: digest polypeptide chain from carboxylic end

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75
Q

3 examples of endopeptidases

A

1) pepsin
2) trypsin
3) chymotrypsin

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76
Q

2 examples of exopeptideases

A

1) carboxypeptidases A & B
2) aminopeptidases

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77
Q

aminopeptidases are ( ) enzymes

A

brush border

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78
Q

aminopeptidases

A

group of protease enzymes produced by enterocytes

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79
Q

enterocytes are ( ) enzymes

A

brush border

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80
Q

exopeptidase digestion end product

A

free AA

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81
Q

endopeptidase digestion end products

A

oligopeptides & small peptides

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82
Q

major absorption pathway for AA in monogastrics

A

facilitated by pept1

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83
Q

PEPT-1

A

hydrogen dependent transport system

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84
Q

passive diffusion of AA

A

via tight junctions

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85
Q

3 AA transporters

A

1) Na dependent
2) H dependent
3) Na independent

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86
Q

ionic gradients of H dependent transport is maintained by the

A

Na pump

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87
Q

4 steps of Na dependent AA transporter

A

1) Na binds to binding site on transporter
2) increases affinity for transporter for AA
3) AA binds to its binding site
4) both Na & AA are transported together into enterocyte & into the cell

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88
Q

why is AA transport through the Na K ATPase pump not the primary pathway?

A

it is an energy dependent process

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89
Q

what enzyme activates trypsinogen to trypsin

A

enteropeptidase

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90
Q

sodium hydrogen exchanger

A

removes H from cell in exchange for Na

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91
Q

what membrane does the Na K ATPase pump operate on?

A

basolateral membrane

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92
Q

why would there be more N in the duodenum than contained in the diet?

A

b/c of endogenous proteins

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93
Q

what N source is most abundant in feces

A

microbial N

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94
Q

microbial N

A

N from growth of microorganism in the hind gut + endogenous proteins

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95
Q

4 major sources of N in a monogastric diet

A

1) microbial N
2) sloughed off epithelial cells
3) enzymes
4) undigested feed nitrogen

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96
Q

what is the major source of N in monogastric diet

A

undigested feed N

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97
Q

why must all endogenous proteins not be lost

A

no growth / production bc losing more N than consuming

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98
Q

2 examples of anti-nutritional factors

A

1) trypsin inhibitor
2) tannins

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99
Q

what do trypsin inhibitors do

A

change shape of trypsin & chymotrypsin = unable to digest proteins

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100
Q

how to remove trypsin inhibitors and tannins from the feed

A

heat

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101
Q

tannins

A

phenolic compounds that bind proteins = reduce solubility of protein = reduced digestion

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102
Q

how are mallard products formed

A

when feed ingredients are heat treated = makes proteins less soluble = reduces digestibility

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103
Q

T or F: mallard reactions are undesirable in monogastrics

A

T

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104
Q

T or F: heat decreases protein solubility

A

T

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105
Q

3 AA used most extensively by small intestine during absorption

A

1) glutamate
2) glutamine
3) aspartate

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106
Q

T or F: lots of glucose is absorbed by small intestine for energy

A

F

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107
Q

glutamate -> a-ketoglutarate is a ( ) reaction

A

transamination

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108
Q

how does the small intestine get energy from glutamate, glutamine & aspartate

A

1) deamination reaction: glutamine -> glutamate
2) transamination reaction: glutamate -> a-ketoglutarate = can now enter TCA cycle for energy

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109
Q

what is used for ureagenesis

A

ammonia

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110
Q

glutamine, glutamate & aspartate are ( ) to produce energy

A

oxidized

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111
Q

glutathione is an

A

antioxidant

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112
Q

what organ is the major use of amino acids? for what function?

A

liver, energy

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113
Q

2 fates of AA

A

1) liver
2) other tissues

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114
Q

what % of amino acids in portal circulation absorbed from the small intestine are used by the liver?

A

50%

115
Q

T or F: protein turnover is continual

A

T

116
Q

rate of protein synthesis is ( ) than rate of protein degradation in animals that are growing

A

higher

117
Q

Ks vs kd

A

Ks- protein synthesis
Kd- protein degradation

118
Q

Ks > Kd =

A

protein accretion

119
Q

when does catabolism of amino acids occur?

A

when carbohydrate intake is limited

120
Q

what 2 catabolic states increase amino acid catabolism

A

sepsis & metabolic acidosis

121
Q

ureagenesis

A

pathway to detoxify ammonia

122
Q

ammonia is toxic to the ( ) system

A

central nervous system

123
Q

how are non-essential amino acids synthesized?

A

transamination reactions

124
Q

3 most active aminotransferases / 3 major players in transamination reactions

A

1) alanine
2) aspartate
3) glutamate

125
Q

alanine gives up amino group to a-ketoglutarate to become

A

glutamate

126
Q

aspartate becomes

A

oxaloacetate

127
Q

alanine becomes

A

pyruvate

128
Q

oxidative deamination

A

amino acid releases amino group to produce ammonia + a-ketoglutarate

129
Q

transamination vs deamination reactions

A

T: no release of free ammonia, occur in lots of diff tissues
D: release of free ammonia, occur mostly in liver

130
Q

2 causes of livestock ammonia toxicity

A

1) overfeed urea
2) genetic defects in urea cycle

131
Q

primary site of catabolism of glutamine & glutamate

A

skeletal muscle

132
Q

transamination of branched chain amino acids in skeletal muscle results in the production of

A

glutamine and glutamate

133
Q

during transamination reaction, glutamine ( ) amino group and glutamate ( ) amino group

A

accepts, donates

134
Q

mechanism that prevents releasing ammonia into the bloodstream

A

alanine glucose cycle

135
Q

alanine glucose cycle

A

1) alanine transports the amino group from skeletal muscle to liver
2) glucose is released by liver -> skeletal muscle -> carbon skeleton of alanine

136
Q

cost of urea synthesis

A

4 high energy phosphate bonds

137
Q

where does the N in urea come from

A

catabolism of AA

138
Q

arginine is important for the resynthesis of

A

orthinine

139
Q

orthinine function

A

limits ability of urea cycle to operate

140
Q

why do diets low in arginine impact the urea cycle?

A

reduces ability to regenerate orthonine which is needed for the urea cycle to operate

141
Q

1 oxaloacetate is used to synthesize ( ) for the production of fumarate

A

aspartate

142
Q

problem with urea excretion

A

urea is very rapidly degraded in the environment = ammonia production

143
Q

ammonotelic refers to what species

A

aquatic species

144
Q

ureotelic refers to what species

A

mammals

145
Q

uricotelic refers to what species

A

birds/reptiles

146
Q

what causes pasty form of bird poop

A

uric acid

147
Q

T or F: there is little loss of water with uric acid excretion

A

T

148
Q

T or F: uricogenic animals require more energy to excrete uric acid

A

T

149
Q

how many ATP are hydrolyzed in ureagenesis

A

4

150
Q

animal that secrete urea have a ( ) proportion of N b/c uric acid is higher in energy costs, therefore ( ) N content

A

higher

151
Q

4 major sources of N in uric acid

A

1) glycine
2) glutamine
3) glutamate
4) aspartate

152
Q

what is required in broiler diets for uric acid synthesis?

A

glycine

153
Q

are plant or animal proteins higher in glycine

A

animal

154
Q

urea is what % N

A

47

155
Q

uric acid is what % N

A

33

156
Q

uric acid synthesis has a ( ) energy cost

A

higher

157
Q

ammonia -> uric acid vs uric acid -> ammonia on water requirements & energy cost

A

a->u : higher energy cost, lower water requirement
u->a: lower energy cost, higher water requirement

158
Q

disposal of carbon skeleton occurs primary through

A

ureagenesis

159
Q

T or F: carbon skeleton from any amino acid can be used to generate energy through the krebs cycle

A

T

160
Q

T or F: some carbon skeletons are used exclusively for glucose synthesis

A

T

161
Q

glucogenic carbon skeletons end up as? (5)

A
  • a-ketoglutarate
  • succinyl CoA
  • fumarate
  • oxaloacetate
  • pyruvate
162
Q

ketogenic carbon skeletons end up as? (2)

A
  • acetyl CoA
  • acetoacetyl CoA
163
Q

phenylalanine is a ( )genic AA

A

glucogenic & ketogenic

164
Q

why it it inefficient to catabolize AA for energy?

A

b/c have to dispose of amino group which costs energy & heat increment increases

165
Q

heat increment definition

A

change in heat production after a meal

166
Q

Kwashiorkor

A

protein deficiency with swelling

167
Q

marasmus

A

protein and energy deficiency, no swelling

168
Q

T or F: marasmus is more severe than kwashiorkor

A

T

169
Q

T or F: protein synthesis is an all or nothing event

A

T

170
Q

T or F: genetics determine an animal’s capacity for lean meat deposition

A

T

171
Q

what is the 1st limiting amino acid in pigs vs poultry

A

pigs- lysine
poultry- methionine

172
Q

2 major factors of protein quality

A

1) AA content determined by sequence/primary structure of AA sequence
2) digestibility of protein -> constituents being released

173
Q

what 2 methods are amino acid requirements based on?

A

1) limiting amino acid requirements
2) ideal protein balance

174
Q

what is a first limiting amino acid?

A

supplied in the least amount in diet relative to an animals requirement
- protein synthesis can only take place to the extent that lysine can support

175
Q

what is the 1st limiting amino acid in monogastrics

A

lysine

176
Q

why is methionine the 1st limiting amino acid in poultry?

A

bc feathers are very high in methionine

177
Q

T or F: without synthetic AA, it is hard to formulate balanced diets for monogastrics

A

T

178
Q

ideal protein balance concept

A

perfect balance of EAA that will meet requirements for maintenance & production but everything is expressed relative to the lysine or the limiting amino acid
- expressed as a % of lysine

179
Q

5 advantages of using the ideal protein concept

A

1) balanced EAA composition
2) maximize growth
3) avoid under-feeding
4) reduces cost of diet
5) less N excretion bc proteins are in proper proportions

180
Q

why is lysine set to 100 in ideal protein

A

only used for protein synthesize

181
Q

T or F: age is a major factor that influences ideal protein ratios

A

T

182
Q

T or F: only lysine is static in ideal protein ratios, the rest are all different

A

T

183
Q

( ) requirements continues to increase to support protein accretion as the animal gets heavier

A

lysine

184
Q

advantage & disadvantage of matching EAA content

A

A: save costs, less AA oxidation
D: difficult to manage

185
Q

why is it called apparent digesibility?

A

bc not accounting for sloughed off epithelial cells & enzymes

186
Q

T or F: apparent digestibility is used to formulate diets

A

F- it is very misleading bc it does not account for endogenous protein losses

187
Q

T or F: microorganisms have lysine requirements

A

T

188
Q

problem with measuring endogenous losses

A

digestive function

189
Q

T or F: apparent fecal & ileal AA digestibility is used to calculate diets

A

F

190
Q

what digestibility calculation is used to formulate diets

A

true ileal AA digestibility

191
Q

2 methods to measure amino acid requirements

A

1) broken line model
2) quadratic model

192
Q

broken line model

A

add more AA until weight gain plateaus
- not biologically correct

193
Q

quadratic model

A

add more AA until find peak in weight gain curve
- decreases are due to toxic effects

194
Q

what is the major source of AA in ruminants vs monogastrics

A

ruminants- microbial protein
monogastrics- dietary protein

195
Q

true proteins + example

A

AA linked by peptide bonds to form large polypeptides
- canola meal

196
Q

2 major sources of NPN in ruminant diet

A

1) urea in diet
2) ammonia in fermented forages

197
Q

urea makes up to (%) of DM in ruminant rations

A

2%

198
Q

major NPN in forages is

A

ammonia

199
Q

degradation of NPN produces

A

ammonia

200
Q

RUP is digested in ( ) to provide ( )

A

small intestine, AA

201
Q

RDP are degraded in the ( ) to provide ()

A

rumen, nitrogenous compounds

202
Q

T or F: microbial proteins require ATP to synthesize microbial proteins

A

T

203
Q

metabolizable protein =

A

microbial protein + RUP

204
Q

3 fates of ammonia in rumen

A

1) absorbed by rumen wall
2) go to bloodstream for excretion as urea
3) recycled back in saliva

205
Q

2 components of dietary protein

A

RUP + RDP

206
Q

true proteins are degraded to

A

AA & small peptides

207
Q

T or F: protein degradation is initially an extracellular process

A

T

208
Q

carbon skeletons from AA are degraded to produce ( ) in ruminants

A

VFAs

209
Q

the process of dietary protein -> amino acid occurs ( ) and small peptides -> VFAs occur ( )

A

extracellularly, intracellularly

210
Q

what % of rumen bacteria are proteolytic

A

30-50

211
Q

difference between bacteria & protozoa

A

bacteria: use ammonia as N source for bacterial protein synthesis
protozoa: major source of N is the bacteria they consume

212
Q

T or F: there is high urease activity in the rumen

A

T

213
Q

T or F: urease is expressed everywhere in the rumen

A

T

214
Q

what is required for microorganisms to use ammonia to synthesize AA?

A

carbon skeleton from VFAs

215
Q

fiber digesting microorganisms prefer( ) as an N source for microbial protein synthesis

A

ammonia

216
Q

coupled fermentation

A

nitrogenous compounds are available at the same time as ATP that drives microbial protein synthesis

217
Q

protozoa preferred source of N is

A

bacteria

218
Q

what is the most efficient protein synthesis in the rumen?

A

coupled fermentation

219
Q

energy sources are fermented to produce

A

ATP

220
Q

sugars are ( ) rapidly fermented than steam flaked corn / ground barley

A

more

221
Q

why add sugars in diet to help with microbial protein synthesis?

A

sugars ferment rapidly like urea so they will ferment together = efficient microbial protein synthesis

222
Q

T or F: rumen ammonia concentration is more stable when ammonia & ATP release are matched

A

T

223
Q

what occurs with uncoupled fermentation

A

protein source is fermented faster than carb source = no ATP available = ammonia is absorbed into bloodstream = wasted N

224
Q

what happens when you maximize microbial protein production

A

minimize RUP

225
Q

3 factors that affect rumen microbial protein production

A

1) rumen NH3 levels
2) available energy
3) AA/peptides

226
Q

How does an acidic rumen affect microbial protein synthesis?

A

suppresses it

227
Q

SF22 effect on microbial N

A

b/c of rapid production of VFA = decrease in rumen pH

228
Q

T or F: rumen NH3 concentration is very dynamic

A

T

229
Q

T or F: forages are quite high in ammonia

A

T

230
Q

T or F: a more fermentable carb = more stable ammonia production in rumen

A

T

231
Q

rumen dilution rate

A

proportion of total volume leaving the rumen per hour

232
Q

faster rumen dilution rate = ( ) outflow of microbial protein

A

more efficient

233
Q

2 reasons why a faster rumen dilution rate causes a greater rate of outflow of microbial protein

A

1) protozoa
- faster = less opportunity to eat bacteria = more will reach small intestine
2) keep more bugs in rumen = can support growth of new organisms

234
Q

protozoa make up (%) of rumen microbial mass

A

20-70%

235
Q

protozoa make up (%) of total rumen N

A

10-40%

236
Q

what % of rumen protozoa wash out to lower gut

A

20-40%

237
Q

T or F: protozoa have small contribution to metabolizable protein

A

T

238
Q

2 main microorganisms responsible for protein degradation

A

1) protozoa
2) bacteria

239
Q

how often do bacteria double their numbers in the rumen?

A

every 60 mins

240
Q

how often do protozoa double their numbers in the rumen?

A

10-60 hours

241
Q

T or F: population density of protozoa are lower than bacteria

A

T

242
Q

2 main problems with protozoa

A

1) not providing AA to the animal by staying in the rumen
2) using up rumen energy

243
Q

2 ways protozoa remain in the rumen

A

1) stick to feed particles
2) attach to rumen epithelium

244
Q

defaunation of protozoa ( ) rumen N efficiency

A

improves

245
Q

what is the universal response to when protozoa are not present in the rumen?

A

rumen ammonia & N concentration decreases

246
Q

what will happen to fiber digestion if there is no protozoa in the rumen?

A

it will decrease bc they are important for fiber digestion

247
Q

2 functions of protozoa in the rumen

A

1) fiber digestion
2) energy

248
Q

how do young ruminants establish a protozoa population?

A

cross inoculation from staying on dam

249
Q

why do feedlot animals not have protozoa in their rumens?

A

high concentrate diet makes protozoa eat too much start and then they explode

250
Q

T or F: unsaturated fats are toxic to protozoa

A

T

251
Q

T or F: ruminants have requirement for microbial protein

A

T

252
Q

3 factors that influence the extent of rumen degradation

A

1) protein structure
2) rumen passage rate
3) rumen pH & diet type

253
Q

how do denatured proteins impact digestibility in monogastrics vs ruminants

A

monogastrics: uncoils & makes more accessible to enzymes
ruminants: reduce solubility in rumen fluid = reduces degradation

254
Q

what makes good sources of RUP?

A

proteins coiled amongst themselves = lowers solubility

255
Q

animal proteins are ( ) undergradable in the rumen compared to plant proteins

A

more

256
Q

why are animal proteins less degradable in the rumen?

A

high in disulfide linkages = less soluble in rumen = less degradable

257
Q

4 factors that limit the use of animal proteins in the diet

A

1) cost
2) availability
3) consumer perceptions
4) CFIA regulations

258
Q

why can meat/bone meal not be fed to ruminants

A

bc of mad cow disease

259
Q

a reduction in particle size = ( ) degradation

A

improved b/c increases surface area

260
Q

optimal pH for proteases

A

5.5-7

261
Q

acidic rumen conditions ( ) protein degradation/ why?

A

decrease, microorganisms responsible for protein degradation are sensitive to acidic conditions

262
Q

2 advantages of lowering protein degradation in the rumen

A

1) lower ammonia production
2) increase rumen by pass protein

263
Q

fermentation is slowed when protein degradation is

A

decreased

264
Q

T or F: mature cows on pasture have no requirement for RUP

A

T

265
Q

low protein diets depend on ( ) to provide N for microbial protein synthesis

A

urea recycling

266
Q

2 methods of ammonia absorption
- do they use NH3 or NH4

A

1) passive diffusion (NH3)
- across rumen wall into bloodstream
2) potassium channels (NH4)
- cannot freely diffuse so must use potassium channels

267
Q

NH3 vs NH4

A

NH3- ammonia
NH4- ammonium

268
Q

3 factors that impact ammonia absorption from the rumen

A

1) rumen ammonia levels
- higher levels = more absorbed
2) ATP supply
- more ATP = lower ammonia concentration
3) rumen pH
- more alkaline pH = more absorption bc ammonia exists in NH3 form = passive diffusion is more rapid

269
Q

3 fates of blood urea

A

1) urine
2) milk
3) liver
4) saliva

270
Q

a high fiber diet will ( ) the amount of urea recycled via saliva

A

increase

271
Q

2 transporters that secrete urea directly into rumen via rumen wall

A

1) urea transporters
2) aquaporins

272
Q

why is ATP required for urea use in the rumen

A

protozoa cannot use urea as a source of N so bacteria need ATP to drive this process

273
Q

as CP increases, the amount of urea that is recycled ( )

A

decreases

274
Q

what % of protein is in a ruminant diet

A

14-16%

275
Q

T or F: more N in the diet will decrease urea recycling

A

T

276
Q

T or F: high ammonia concentration in the rumen has inhibitory effects on urea recyling

A

T

277
Q

impacts on urea recycling in high vs low blood urea concentrations

A

high= facilitate movement of urea into the blood
low= less urea moved

278
Q

T or F: any microbial protein production in large intestine will not provide energy

A

T

279
Q

what animals will benefit from microbial protein production in the large intestine

A

rabbits -> coprophagy

280
Q

2 disadvantages to rumen protein degradation

A

1) rumen microbes are proteolytic = degrade any N compounds = waste
2) most dietary N is absorbed as NH3, not as AA = not useful to animal
- also need to detoxify via ureagenesis which costs ATP

281
Q

monogastric vs ruminant source of essential AA

A

monogastrics: dietary protein
ruminants: microbial protein + RUP

282
Q

a-ketoglutarate is the alpha-keto acid of

A

glutamate

283
Q

T or F: ruminants do not have dietary requirement for essential amino acids

A

T- required but do not have to be supplied in the diet

ANSC 315 (9 decks)

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