ANSC 303 - Exams 4 - Proteins

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98 Terms

1
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What are proteins made of?

Amino acids.

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What does EAA stand for?

Essential amino acids.

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What does NEAA stand for?

Non-essential amino acids.

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What mnemonic is used in the notes for essential amino acids?

MATT HILL UP.

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Which essential amino acid contains sulfur?

Methionine.

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What are the essential amino acids listed in the notes?

Methionine, arginine, threonine, tryptophan, histidine, isoleucine, leucine, lysine, valine, and phenylalanine.

7
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Why are essential amino acids required in the diet?

They are not synthesized by the body at a fast enough rate to meet requirements.

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How must essential amino acids be supplied to optimize animal performance?

They must be absorbed from the small intestine in proper quantities.

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Why can essential amino acids be expensive?

They must be supplied in the diet because the body cannot make enough of them.

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What happens to excess amino acids when they are overfed?

They can be made into glucose or used for energy.

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What are non-essential amino acids?

Amino acids synthesized by the body in sufficient amounts to meet the animal's requirements.

12
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Are non-essential amino acids required for normal metabolism?

Yes.

13
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Why do ruminants generally not need essential amino acids supplied directly in the diet?

Ruminal microbes have the capacity to synthesize all amino acids.

14
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Do ruminants still require essential amino acids to be absorbed from the small intestine?

Yes.

15
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What do ruminal microbes require to make amino acids?

A carbon skeleton, volatile fatty acids (VFA), ammonia (NH3), ATP, and building equivalents (BE).

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What is the general sequence for microbial amino acid and protein synthesis in the notes?

Carbon skeleton + VFA + ammonia + ATP + BE → amino acids + ATP + BE → microbial crude protein (MCP).

17
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Which type of cattle may require essential amino acids in excess of what microbes can synthesize?

High-producing dairy cows.

18
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Which essential amino acid is specifically important for high-producing dairy cows?

Methionine.

19
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Why is methionine important in high-producing dairy cows?

It supports greater milk production.

20
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How can methionine be protected in the rumen?

Protect it from microbial degradation.

21
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What other type of cattle may require essential amino acids in excess of microbial synthesis?

Implanted growing steers grazing on wheat.

22
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What protein source is supplied to implanted growing steers grazing on wheat?

Ruminal undegradable protein (RUP).

23
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What are maintenance amino acid requirements?

The amino acid requirements needed to maintain the animal.

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How do maintenance requirements change as animal size increases?

They increase.

25
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How do maintenance requirements change as lean muscle size increases?

They increase.

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How do maintenance requirements change with age?

They decrease as age increases.

27
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How do amino acid requirements relate to production potential?

They increase as production potential increases; for example, a high-producing dairy cow has greater requirements than a beef cow.

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What is a peptide bond?

A bond between two amino acids.

29
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What is released when a peptide bond forms?

Water (H2O).

30
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What enzyme forms peptide bonds according to the notes?

A proteolytic enzyme (peptidase).

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What is a polypeptide?

A chain containing more than 10 amino acids.

32
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How many amino acids and peptide bonds are in a tripeptide?

Three amino acids and two peptide bonds.

33
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How many amino acids and peptide bonds are in a dipeptide?

Two amino acids and one peptide bond.

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How many amino acids and peptide bonds are in a single amino acid?

One amino acid and zero peptide bonds.

35
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What are amino acids, dipeptides, and tripeptides in relation to small-intestinal digestion?

They are products of digestion and are absorbed by the small intestine.

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What is the primary structure of a protein?

The sequence of amino acids.

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What is the secondary structure of a protein?

Hydrogen bonding between amino acids.

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What is the tertiary structure of a protein?

Clustering of hydrophobic regions.

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What is the quaternary structure of a protein?

Interaction between polypeptides.

40
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What does HCl in the stomach do to proteins?

Denatures proteins.

41
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Which protein structures are affected by denaturation?

Secondary, tertiary, and quaternary structures (2°, 3°, and 4°).

42
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What breaks peptide bonds during protein digestion?

Enzymatic hydrolysis.

43
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What are the three main stages of non-ruminant protein digestion?

Denaturation, enzymatic hydrolysis of peptide bonds, and absorption.

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What happens during protein denaturation in a non-ruminant?

Stomach acid exposes peptide bonds for enzymatic digestion.

45
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Where does enzymatic hydrolysis of peptide bonds occur?

In the stomach and small intestine.

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Which protein structure is affected by enzymatic hydrolysis of peptide bonds?

Primary structure (1°).

47
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What protein digestion products are absorbed?

Dipeptides, tripeptides, and amino acids.

48
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What happens to food in the mouth during protein digestion?

Particle size is decreased.

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What does HCl do in the stomach during protein digestion?

It decreases pH and denatures proteins, affecting structures 2°, 3°, and 4°.

50
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What is a zymogen?

An inactive enzyme precursor.

51
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Why is pepsinogen kept in an inactive state?

If active, it could digest the organs where it is produced.

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What activates pepsinogen?

HCl or pepsin.

53
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What enzyme is formed when pepsinogen is activated?

Pepsin.

54
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How is pepsinogen activation described in the notes?

HCl activation is reversible; pepsin activation is irreversible.

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What does pepsin do?

Hydrolyzes peptide bonds.

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Where is pepsinogen made?

In the stomach.

57
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Where does pepsin act?

In the stomach.

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What type of enzyme is pepsin?

An endopeptidase.

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Where is trypsinogen made?

In the pancreas.

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What activates trypsinogen?

Enteropeptidase or trypsin.

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What enzyme is formed from trypsinogen?

Trypsin.

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Where does trypsin act?

In the small intestine.

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What type of enzyme is trypsin?

An endopeptidase.

64
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Where is chymotrypsinogen made?

In the pancreas.

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What activates chymotrypsinogen?

Trypsin.

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What enzyme is formed from chymotrypsinogen?

Chymotrypsin.

67
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Where does chymotrypsin act?

In the small intestine.

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What type of enzyme is chymotrypsin?

An endopeptidase.

69
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Where is procarboxypeptidase made?

In the pancreas.

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What activates procarboxypeptidase?

Trypsin.

71
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What enzymes are formed from procarboxypeptidase?

Carboxypeptidases A and B.

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Where do carboxypeptidases A and B act?

In the small intestine.

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What type of enzyme are carboxypeptidases A and B?

Exopeptidases.

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What does an endopeptidase do?

Hydrolyzes peptide bonds within the interior of a protein.

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What does an exopeptidase do?

Hydrolyzes peptide bonds at the exterior of a protein.

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Where is enteropeptidase produced?

By the enterocyte.

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What does enteropeptidase activate?

Trypsinogen.

78
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Which hormones are noted as signals associated with release of digestive secretions?

CCK and secretin.

79
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What are brush border enzymes (BBE)?

Peptidases.

80
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What does aminopeptidase do?

Cleaves one amino acid from oligopeptides.

81
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What does dipeptidylaminopeptidase do?

Cleaves dipeptides from oligopeptides.

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What does tripeptidase do?

Cleaves one amino acid from a tripeptide.

83
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What does RUP stand for?

Ruminal undegradable protein; also called undegradable intake protein (UIP).

84
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What is RUP?

The fraction of protein that ruminal microbes cannot degrade.

85
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What happens to the amino acid profile of RUP as it leaves the rumen?

It leaves with the same amino acid profile as the feed.

86
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What digestibility value is given for RUP in the notes?

80% digestible (the notes indicate a range of 0%–100%).

87
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What does RDP stand for?

Ruminal degradable protein; also called degradable intake protein (DIP).

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What happens to RDP in the rumen?

The notes state that 100% of RDP is degraded.

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How do ruminal microbes use RDP?

They use it to synthesize microbial crude protein (MCP).

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What happens to the amino acid profile of RDP?

Ruminal microbes alter the amino acid profile.

91
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What can RDP supply or generate in relation to non-protein nitrogen (NPN)?

Urea, ammonia, and amino acids.

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What determines the ratio of RUP to RDP in a feedstuff?

The feedstuff and its passage rate (Kp).

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What happens to RDP and RUP when Kp increases?

RDP decreases and RUP increases because retention time is shorter.

94
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What happens to RDP and RUP when Kp decreases?

RDP increases and RUP decreases because retention time is longer.

95
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What does RDP supply for microbial crude protein synthesis?

Ammonia (NH3).

96
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What can excess ammonia indicate in relation to RDP?

RDP may be supplied in excess of microbial needs.

97
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Why is RDP fed to ruminants?

To meet microbial requirements so microbes can synthesize cells and enzymes.

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What happens when RDP is limited?

Carbohydrate fermentation is prevented or reduced, decreasing the energy available to the cow.