Test 3 Flashcards

1
Q

What are lipids?

A

Organic compounds that contain C, H, and O

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2
Q

Do lipids have more hydrogen or less hydrogen that CHOs? More or less oxygen?

A

More

Less

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3
Q

How much more energy is in lipids than CHOs?

A

2.25 times more

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4
Q

How many calories should come from fat?

A

Less than 30%

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5
Q

What is the structure of lipids?

A

CH3(CH2)x–COOH

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6
Q

What part of lipids is polar?

A

Carboxylic acid (COOH)

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7
Q

What is a short chain lipid? Examples?

A

Less than 14 carbons

Acetate, Butyrate, Propionate

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8
Q

What is an example of a long chain lipid?

A

Fatty acid chains

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9
Q

What is a saturated fatty acid?

A

No double bond

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10
Q

What are fatty acids saturated with?

A

Hydrogen

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11
Q

What are some saturated fatty acids? What is the carbon to unsaturated points ratio for each?

A

Myristate: C14:0

Palmitate: C16:0

Stearate: C18:0

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12
Q

What is an unsaturated fatty acid?

A

It has pi bonds and loses 2 hydrogens

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13
Q

What are some unsaturated fatty acids? What is the carbon to unsaturated points ratio for each?

A

Palmitoleic: C16:1

Oleic: C18:1

Linoleic: C18:2

Linolenic: C18:3

Arachidonic: C20:4

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14
Q

What is an essential fatty acid?

A

Can’t be synthesized by body, therefore it is a dietary requirement

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15
Q

What are the essential fatty acids?

A

Linoleic

Linolenic

Arachidonic (cats)

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16
Q

What is triacylglycerol composed of?

A

Glycerol and 3 fatty acids

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17
Q

Look at the structure of triacylglycerol on page 54

A

Look at the structure of triacylglycerol on page 54

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18
Q

What do the following suffixes mean for fatty acids?

Di-

Mono-

Phospho-

Glyco-

Sulfo-

A

2 fatty acids

1 fatty acid

Phosphate group

Carbohydrate group

Sulfate group

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19
Q

What is a lipoprotein?

A

A lipid that contains protein (cholesterol)

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20
Q

What is a low density lipoprotein?

A

High in lipid, low in protein (bad cholesterol)

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21
Q

What is a high density lipoprotein?

A

Low in lipid, high in protein (good cholesterol)

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22
Q

What are waxes?

A

Esters of fatty acids and long chain alcohols that are not digestible

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23
Q

What are steroids like in water?

A

Insoluble in water

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24
Q

Look at the basic structure of a steroid on page 55

A

Look at the basic structure of a steroid on page 55

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25
Q

What is cholesterol?

A

Precursor for sex hormones

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26
Q

What are carotenoids? Example?

A

Vitamin A precursor

Carotene – yellow pigment of veggies

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27
Q

What is the goal of digestion in monogastric animals?

A

To turn triacylglycerol into monoglyceride and 2 fatty acids which are then absorbed

Triacylglycerol is insoluble and must become soluble

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28
Q

What are the 9 steps in digestion and absorption of monogastric animals?

A
  1. Course emulsion is formed (fat globule)
  2. Bile acts to form droplet in duodenum
  3. Lipase acts at fat:water interface and cleaves FA 1 and 3
  4. Micelles are formed
  5. Upon contact with microvilli in duodenum, monoglyceride and free fatty acids are absorbed
  6. As absorbed, monoglycerides and fatty acids are immediately resynthesized to triacylglycerol and phospholipids
  7. Triacylglycerol droplets enveloped by lipoprotein chylomicron and exits cells to lymph system
  8. Glycerol is passively absorbed
  9. Short chain fatty acids are absorbed without chylomicron and go to the blood. If fatty acid 2 is short chain, it goes to lymph
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29
Q

Look at page 59 under examples

A

Look at page 59 under examples

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30
Q

What happens to fatty acids in post absorption in monogastric animals?

A

Stored as fat in adipose tissue (constant turnover) Converted to acetyl CoA via β oxidation

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31
Q

Is β oxidation aerobic or anaerobic?

A

Aerobic–mitochondria

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32
Q

What is β oxidation?

A

Break down of fat to acetyl CoA

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33
Q

What is 1 cycle of β oxidation like?

A
  1. Takes off 2 carbons from acetyl CoA and gives 12 ATP
  2. 1 FADH2 (2 ATP)
  3. 1 NADH (3 ATP)
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34
Q

How many ATP does it take to activate β oxidation?

A

2

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35
Q

What is caproic acid’s carbon to unsaturated points ratio and formula?

A

C6:0 C6H12O2

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36
Q

How many times does caproic acid go through β oxidation?

A

2

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37
Q

How many ATP does caproic acid yield?

A

44

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38
Q

What is stearic acid’s carbon to unsaturated points ratio?

A

C18:0

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39
Q

How many times does stearic acid go through β oxidation?

A

8

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40
Q

How many ATP does stearic acid yield?

A

146

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41
Q

What can Acetyl CoA go to in ketosis?

A

Krebs, Acetoactetate (then acetone), and β-hydroxybutyrate

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42
Q

What are 4 clinical signs of ketosis?

A

High blood ketone level

High urine ketone level

Low blood glucose

Breath smells like acetone

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43
Q

What are 3 causes of ketosis?

A

Body is dependent upon gluconeogenesis (depletes oxaloacetate)

Body mobilizing stored fat (β oxidation –> increase acetyl CoA)

Acetyl CoA –> ketone bodies

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44
Q

When does ketosis occur?

A

Starvation

High producing dairy cow

Late pregnant ewe with twins or triplets

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45
Q

How can you treat ketosis?

A

Increase oxaloacetate precursors

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46
Q

What do the following oxaloacetate precursors become?

Propionate

Gultamate

Aspartate

A

Succinyl CoA

α-ketogutarate

Oxaloacetate

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47
Q

What is fatty acid synthesis similar to?

A

Reverse β oxidation

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48
Q

What happens in fatty acid synthesis with Acetyl CoA?

A

2 carbons are added to Acetyl CoA to get fatty acids

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49
Q

What is the first thing that enters fatty acid synthesis? What does the remaining stuff enter as?

A

Acetyl CoA

Malonyl CoA

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50
Q

How many carbons does Malonyl CoA have?

A

3

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51
Q

What is the basic idea of what happens in fatty acid synthesis? (In terms of the different CoA’s)

A

Malonyl CoA links to Acetyl CoA to get Acyl CoA

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52
Q

For every Malonyl CoA, how many ATP do you need? NADPH? What 2 other things are needed?

A

1

2

biotin and CO2

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53
Q

What is the reaction for palmitic acid?

A

8 Acetyl CoA + 7 ATP + 14 NADPH –> Palmitic acid + 8 CoASH + 14 NADP + 7 ADP (Biotin and CO2 over arrow)

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54
Q

Look at the reactions on page 62 of Acetyl CoA and Malonyl CoA

A

Look at the reactions on page 62 of Acetyl CoA and Malonyl CoA

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55
Q

How many carbons can a fatty acid have for the body to synthesize?

A

18 or less

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56
Q

What is the goal of fatty acid synthesis in ruminant animals?

A

To make triacylglycerol become 3 fatty acids and glycerol (propionate is absorbed)

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57
Q

In the rumen, what do free fatty acids attach to?

A

Fiber particles

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58
Q

What do free fatty acids do in the rumen?

A

Block cellulase from attacking β 1,4 bonds

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59
Q

What is the 5 step process of digestion and absorption in ruminant animals?

A
  1. TG is released from fiber particles in acid of abomasum
  2. Bile in duodenum
  3. Formation of micelle
  4. Absorbed
  5. Chylomicron goes to lymph (most absorbed fatty acids go to adipose)
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60
Q

What is the redox state of the rumen?

A

Highly reduced

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61
Q

What happens to unsaturated fatty acids in the rumen? What percentage does this happen to?

A

They become saturated

60%

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62
Q

What does 2/3 of fatty acids become in beef fat?

A

Stearic acid

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63
Q

What 3 fatty acids become stearic acid?

A

Linoleic

Linolenic

Oleic

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64
Q

How many different proteins are in the body?

A

about 100,000

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65
Q

How much of the body is protein on a dry fat free basis?

A

80%

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66
Q

What are the 3 functions of protein?

A

Structural (skeletal muscle, connective tissue, protective protein)

Specialized functions (enzymes, hormones, blood proteins)

Energy (AA converted to krebs cycle intermediates)

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67
Q

What is the composition of proteins?

A

Carbon, hydrogen, oxygen, and nitrogen. Some have sulfur and/or phosphorus

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68
Q

What does Kjeldahl N allow?

A

To measure nitrogen content

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69
Q

How do you find % crude protein?

A

% N x 6.25

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70
Q

What is true protein comprised of?

A

Amino acids

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71
Q

What do dietary amino acids become?

A

AA in intestinal lumen which become AA in blood which become tissue protein

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72
Q

Why do we eat protein?

A

Because our body needs amino acids

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73
Q

How many amino acids are we concerned with?

A

20

74
Q

Look at the general structure of amino acids on page 65

A

Look at the general structure of amino acids on page 65

75
Q

What is the most reactive part of the amino acid?

A

α carbon

76
Q

What does the R group do on amino acids?

A

Gives individuality to the different amino acids

77
Q

What are the 2 properties of amino acids?

A

Carboxyl group

Amino group

78
Q

What kind of properties do carboxyl groups have?

A

Acid (donates H in solution)

79
Q

What kind of properties do amino groups have?

A

Base (accepts H in solution)

80
Q

How do you get an amino acid to act like an acid or base?

A

Dissolve it in neutral solution

81
Q

What are the different chemical methods of classification?

A

Neutral

Acidic

Basic

Sulfur

Aromatic

82
Q

What are the 9 neutral amino acids?

A

Glycine

Alanine

Valine

Leucine

Isoleucine

Serine

Threonine

Glutamine

Asparagine

83
Q

What are the 2 acidic amino acids?

A

Aspartic Acid

Glutamic Acid

84
Q

What are the 3 basic amino acids?

A

Histidine

Arginine

Lysine

85
Q

What are the 3 sulfur containing amino acids?

A

Cysteine

Cystine

Methionine

86
Q

What are the 3 aromatic amino acids?

A

Phenylalanine

Tyrosine

Tryptophan

87
Q

What are essential amino acids?

A

Amino acids that can’t be synthesized by the body at a rate that can meet the body’s requirements. They are required in the diet

88
Q

What are the 10 essential amino acids?

A

Phenylalanine

Valine

Threonine

Tryptophan

Isoleucine

Methionine

Histidine

Arginine

Leucine

Lysine

89
Q

What are nonessential amino acids?

A

Can be synthesized by the body at an appreciable rate

90
Q

What happened in the 1930s by Dr. Rose?

A

He was the first to classify essential and nonessential amino acids with his model of the growing rat

91
Q

How many amino acids are required by ruminant animals?

A

None

92
Q

What are peptides?

A

Covalent bonds that link amino acids between the –COOH of one amino acid to the NH3 of another

93
Q

What is a dipeptide?

A

2 amino acids linked together

94
Q

How long is a peptide?

A

Usually 3-8 amino acids long

95
Q

How long is a polypeptide?

A

Longer than 8 amino acids

96
Q

How much ATP does it cost to get peptide bonds?

A

4

97
Q

What is the function of protein dependent on?

A

3D structure which is dependent on the sequence of amino acids

98
Q

What determines the function of proteins?

A

Amino acids

99
Q

What are disulfide bonds important for?

A

Maintaining protein structure

100
Q

What are the terminal ends?

A

Glycine and Cysteine

101
Q

What is glycine?

A

Amino terminal amino acid

102
Q

What is cysteine?

A

Carboxyl terminal amino acid

103
Q

What is the primary part of the structure of proteins?

A

The amino acid sequence

104
Q

What does the secondary part of protein structure involve?

A

Bonding with disulfide bonds

105
Q

What is the 3° part of the structure of proteins?

A

The 3D shape

106
Q

What is the 3D shape of proteins caused by?

A

Hydrophobic amino acids

Hydrophilic amino acids

107
Q

What types of amino acids are hydrophobic?

A

Neutral and aromatic

108
Q

What types of amino acids are hydrophilic?

A

Acid and base

109
Q

Where in the protein do hydrophobic amino acids go?

A

Inside

110
Q

Where in the protein do hydrophilic amino acids go?

A

Outside

111
Q

What is denaturing?

A

Irreversible unfolding of protein

112
Q

What are the methods of denaturing?

A

Heat

Chemical

Decrease pH (HCl)

113
Q

What is the goal of protein digestion in monogastric animals?

A

Break protein down to amino acids for absorption

114
Q

What does HCl do? Where does it come from?

A

Denature protein and activate pepsinogen

Parietal cells

115
Q

Where does pepsinogen come from?

A

Chief cells

116
Q

What type of enzyme is pepsinogen?

A

Proteolytic

117
Q

What type of peptidase is pepsinogen?

A

Endopeptidase

118
Q

What does an Endopeptidase do?

A

Cleaves peptide bond in amino acid sequence

119
Q

What are the pancreatic enzymes?

A

Trypsin
Chymotrypsin

Carboxypeptidase

120
Q

Which pancreatic enzymes are Endopeptidases? Exopeptidase?

A

Trypsin and chymotrypsin

Carboxypeptidase

121
Q

What are the duodenal enzymes?

A

Enterokinase amino peptidase

Dipeptidase

122
Q

Look at protein digestion picture on page 74

A

Look at protein digestion picture on page 74

123
Q

How many carrier systems are there?

A

At least 5

124
Q

Why is a carrier system used?

A

To get amino acids across mucosal cell membrane

125
Q

What are the 2 processes of protein synthesis?

A

Transcription and translation

126
Q

What is transcription?

A

DNA is used to make mRNA which ends up in the cytoplasm

127
Q

Where does translation occur?

A

On ribosomes in endoplasmic reticulum

128
Q

What is mRNA a “recipe” for?

A

Protein amino acid sequence

129
Q

What is mRNA divided into? What do they do?

A

Codons (3 base pairs)

Code for a specific amino acid

130
Q

What does tRNA do?

A

Carry specific amino acids to ribosomes for protein synthesis

131
Q

What does turnover refer to?

A

Constant protein turnover that is energy demanding

132
Q

What is turnover a part of?

A

Maintenance energy requirement

133
Q

When does protein synthesis stop?

A

When a specific amino acid is not available when the ribosome needs it

134
Q

What is the limiting amino acid concept based on?

A

Deficiency of one essential amino acid

135
Q

What are four things that are considered catabolism or are catablized?

A

Constant body turnover

Amino acids in excess of requirements

Non-limiting amino acids

Amino acids for energy production

136
Q

What is deamination?

A

Removal of amino group as ammonia

137
Q

What is the general reaction for deamination?

A

Amino acid –> Keto Acid + NH3

(enzyme over arrow/water under arrow)

138
Q

What is transamination?

A

Transfer of amino group from one compound to another

139
Q

What is the general reaction for transamination?

A

Amino acid 1 + Keto Acid 2 –> KA1 + AA2

(enzyme over arrow/ Vit. B6 under arrow)

140
Q

What do ketogenic amino acids become?

A

Acetyl CoA

141
Q

What are the 3 ketogenic amino acids?

A

Leucine, isoleucine, and phenylalanine

142
Q

What are the gluconeogenic amino acids?

A

All other amino acids that aren’t ketogenic and phenylalanine

143
Q

Look at page 78 and 79

A

Look at page 78 and 79

144
Q

What amino acids come in to the krebs cycle with pyruvate? (5)

A

Alanine

Cysteine

Glycine

Serine

Threonine

145
Q

What amino acids come into the krebs cycle with Acetyl CoA? (3)

A

Isoleucine

Leucine

Tryptophan

146
Q

What amino acids come in to the krebs cycle with acetoacetate? (5)

A

Leucine

Lysine

Phenylalanine

Tyrosine

Tryptophan

147
Q

What amino acids come in to the krebs cycle with glutamate (becomes α-ketoglutarate)? (4)

A

Arginine

Glutamine

Histidine

Proline

148
Q

What amino acids come into the krebs cycle with Succinyl CoA? (3)

A

Isoleucine

Methionine

Valine

149
Q

What amino acids come into the krebs cycle with fumarate? (2)

A

Phenylalanine

Tyrosine

150
Q

What amino acids come into the krebs cycle with oxaloacetate? (2)

A

Aspartate

Asparagine

151
Q

What are the 7 symptoms of ammonia toxicity?

A

Muscle tremors

Slurred speech

Blurred vision

Ataxia, inccordination

Tetany, violent spasms

Comotose state

Death- acute 30 minutes, or could take days

152
Q

What are the 4 steps of the urea cycle?

A
  1. Ammonia detoxification
  2. Nitrogen for urea synthesis enters as NH3 from deamination
  3. Requires 4 high energy phosphate bonds per urea molecule
  4. Fate of urea in blood (blood urea nitrogen):

Urine, rumen (via saliva), and cecum

153
Q

What places in the body recycle urea?

A

Rumen and cecum

154
Q

Can birds produce urea?

A

No

155
Q

What do birds use as excretory product?

A

Uric acid which requires glycine

156
Q

What do ruminants do with urea?

A

Recylce it to rumen (horses to cecum)

157
Q

What does bacteria do in ruminant protein digestion?

A

Secrete protease which is eventually broken down to NH3 and a carbon skeleton

158
Q

What is microbial protein?

A

Protein synthesized by microbes

159
Q

What does nonprotein nitorgen (urea) use to make amino acids?

A

NH3 and carbon skeleton

160
Q

What does feeding nonprotein nitrogen help do?

A

Meet tissue amino acid requirements

161
Q

What does an escape protein do or not do?

A

It does not undergo ruminal degradation

162
Q

What does heating the protein source of escape proteins do?

A

Decrease solubility which decreases the ability to be broken down

163
Q

Place the following in decreasing order of escape protein amounts: SBM, fishmeal, grass.

A

Grass < SBM < Fishmeal

164
Q

What is the purpose of NH3 and a carbon skeleton?

A

NH3 is produced rapidly and a carbon skeleton is needed at the same time

165
Q

When is nonprotein nitrogen beneficial?

A

When proper CHO’s are also fed

166
Q

Why are urea and hay not a good match for a diet?

A

Urea is a protein source, hay is a carbon energy source. Urea will be absorbed by kidney and the animal will urinate on the ground because fiber (cellulose) is not digested quickly

167
Q

What does microbial protein come from?

A

Nonprotein nitrogen and soluble protein in the diet

168
Q

What are amino acids available to tissue from?

A

Escape and microbial protein

169
Q

Look at page 86

A

Look at page 86

170
Q

Why can ruminants survive with low protein?

A

Becuase of urea and recycling

171
Q

Why do ruminants and humans not compete for food?

A

Because of nonprotein notrogen and met amino acid requirements

172
Q

Where are microbial and escape proteins digested and absorbed at?

A

Small intestine

173
Q

In adult ruminants, what can protein requirements be met with?

A

100% microbial protein

174
Q

In young or lactating ruminants, what can protein requirements be met with?

A

75% microbial proteins

25% escape proteins

175
Q

How can you decrease protein solubility?

A

Heat

Coat with fat so bacteria can’t get to it

Chemically treat with formaldehyde

176
Q

What is the biological value of egg protein?

A

95

177
Q

What is the biological value of milk protein?

A

90

178
Q

What is the biological value of meat protein?

A

90

179
Q

What is the biological value of SBM protein?

A

75

180
Q

What is the biological value of meat and bone meal?

A

70

181
Q

What is the biological value of cereal grain?

A

60

182
Q

What is the biological value of microbial protein?

A

75-80