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ZOOTH 212 (Animal Nutrition) > Protein in Animal Nutrition > Flashcards

Protein in Animal Nutrition Flashcards

1
Q

are complex organic nitrogenous compounds made up of amino acids.

A

proteins

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2
Q

proteins contain of what elements?

A

° carbon
° hydrogen
° oxygen
° nitrogen
° sulphur
° phosphorus

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3
Q

how many percent nitrogen that proteins contain?

A

16 percent nitrogen

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4
Q

are amphoteric in nature and exist as dipolar ions in aqueous solution.

A

amino acids

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5
Q

have a basic amino group and an acidic carboxyl group.

A

amino acids

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6
Q

are hydrolyzed by enzymes, acids or alkalies into amino acids.

A

proteins

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7
Q

isoelectric point for a given amino acid at which it is electrically neutral.

A

pH value

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8
Q

amino acids classified into three groups, namely:

A

° aliphatic
° aromatic
° heterocyclic

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9
Q

7 mono amino-mono carboxylic acids (neutral amino acids)

A
  1. glycine
  2. alanine
  3. serine
  4. threoninen
  5. valine
  6. leucine
  7. isoleucine
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10
Q

it is the simplest of the amino acids

A

glycine

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11
Q

2 mono-amino carboxylic acid (acidic amino acid)

A
  1. aspartic acid
  2. glutamic acid
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12
Q

3 Di-amino mono carboxylic acids (basic amino acids)

A
  1. Lysine
  2. Arginine
  3. Citrulline
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13
Q

2 Sulphur containing amino acids

A
  1. Methionine
  2. Cysteine
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14
Q

2 Aromatic Amino Acids

A
  1. Phenyl alanine
  2. Tyrosine
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15
Q

2 heterocyclic amino acids

A
  1. histidine
  2. proline
  3. hydroxyproline
  4. tryptophane
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16
Q

Classification of amino acids

A

° Aliphatic Amino Acids
° Aromatic Amino Acids
° Heterocyclic Amino Acids

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17
Q

What are the Non polar aliphatic amino acids (A.A)

A

° Glycine
° Alanine
° Valine
° Leucine
° Isoleucine
° Methionine

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18
Q

What are the Polar uncharged A.A?

A

° Proline
° Serine
° Threonine
° Asparagine
° Glutamine
° Cysteine

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19
Q

what are the Aromatic Side Chain A.A?

A

° Phenyl alanine
° Tyrosin
° Tryptophane

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20
Q

Functions of proteins

A

° it is essential for the growth and development of the body
° help in maintaining the loss of body tissues and muscles
° they also supply energy to the body

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21
Q

one needed by the animal that cannot be synthesized by the animal in the amounts needed.

A

essential amino acid

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22
Q

one needed by the animals that can be formed from other amino acids by the animals.

A

non-essential amino acid

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23
Q

what are the essential amino acid?

A

° arginine
° histidine
° iso-leucine
° leucine
° lysine
° *methionine
° phenylalanine
° threonine
° tryptohan
° valine

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24
Q

what are the non-essential amino acids?

A

° alanine
° aspartic acid
° citrulline
° cystine
° glutamic acid
° glycine
° proline
° hydroxyproline
° serine
° tyrosine

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25
Q

amino acids which are never found as constituents of proteins but which either play metabolic roles occur as natural products.

A

non protein amino acids

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26
Q

amino acid which is present in a protein in the least amount in relation to be animal’s need.

A

limiting amino acid

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27
Q

livestock in definite proportions requires the essential amino acids.

A

limiting amino acid

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28
Q

the limiting amino acid of corn

A

lysine

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29
Q

can be considered under four basic heading: primary structure, secondary structure, tertiary structure and quaternary structure.

A

Structure of proteins

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30
Q

4 Structure of Proteins

A
  1. Primary structure
  2. Secondary structure
  3. Tertiary structure
  4. Quaternary structure
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31
Q

structure that proteins are built up from amino acids means of a linkage between the a-carboxyl of one amino acid

A

primary structure

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32
Q

refers to the sequence of amino acid along the polypeptide chains of protein.

A

primary structure

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33
Q

structure that peptide chain exist in the form of a right-handed-helix.

A

secondary structure

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34
Q

structure which describes how the chains of the secondary structure further interact through the R-groups of amino acid residues.

A

Tertiary structure

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35
Q

structure that contain more than one polypeptide chain

A

quaternary structure

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36
Q

what are the classification of proteins?

A

I. Fibrous Proteins
II. Globular Proteins
III. Conjugated Proteins
IV. Derived Proteins

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37
Q

these proteins are insoluble and very resistant to animal digestive enzymes

A

fibrous proteins

38
Q

3 types of fibrous proteins

A

a. collagens
b. elastin
c. keratins

39
Q

main proteins of connective tissues.

A

collagens

40
Q

protein found in elastic tissues such as tendon and arteries.

A

elastin

41
Q

protein of hair, hoof, nails etc.

A

keratins

42
Q

important component of collagens

A

hydroxyproline

43
Q

contain about 4 percent sulphur

A

wool protein

44
Q

this group includes all the enzymes, antigens and hormones that are protein.

A

Globular Proteins

45
Q

4 Globular Proteins

A

a. albumin
b. globulins
c. histones
d. protamines

46
Q

water-soluble and heat coagulable and occurs in eggs, milk, blood and many plants.

A

albumin

47
Q

present in eggs, milk and blood and are the main reserve protein source in seed.

A

globulins

48
Q

are basic protein, which occur in cell nucleus where they are associated with DNA.

A

Histones

49
Q

are basic protein of relatively low molecular weight, which are associated with nucleic acid.

A

protamines

50
Q

are composed of simple protein combined with some nom-protein substances as prosthetic group.

A

conjugated proteins

51
Q

4 conjugated proteins

A

a. phosphoprotein
b. glycoprotein
c. lipoprotein
d. chromoprotein
e. nucleoprotein
f. metalloproteins

52
Q

protein’ which on hydrolysis yields phosphoric acid and amino acids.

A

phosphoprotein

53
Q

casein of milk and phosvitin of egg yolk

A

phosphoproteins

54
Q

conjugated proteins with one or more heterosaccharides as prosthetic groups.

A

glycoproteins

55
Q

proteins conjugated with lipid lecithin and cholesterol

A

lipoproteins

56
Q

contain pigment as a prosthetic group.

A

chromoprotein

57
Q

are compound of high molecular weight and conjugated with nucleic acid

A

nucleoproteins

58
Q

a large group of enzyme proteins comtain metallic elements, such as Fe, Co, Mn, Zn, Cu, Mg, etc.

A

metalloproteins

59
Q

this class of proteins includes those substances formed from simple and conjugated proteins.

A

derived proteins

60
Q

2 derived proteins

A
  1. Primary derived proteins
  2. Secondary derived proteins
61
Q

not classed as proteins occur in plants and animals

A

non-protein nitrogenous compounds

62
Q

high molecular weight compounds which, on hydrolysis yield a mixture of basic nitrogenous compound a pentose and phosphoric acid

A

nucleic acid

63
Q

they are carbohydrates derivatives in which purines and pyrimidines found in the nucleic acids.

A

Nucleosides and nucleotides

64
Q

AMP stands for?

A

adenosine monophosphate

65
Q

ADP stands for?

A

adenosine diphosphate

66
Q

ATP stands for?

A

adenosine triphosphate

67
Q

softens the food particles, which is helpful for ingestion of protein.

A

saliva

68
Q

there is no digestion of protein in the mouth because saliva has no proteolytic enzyme

A

Digestion of Protein in Non-ruminants

69
Q

are the most important peptic enzymes of the stomach.

A

pepsi and gastricin

70
Q

secrete hydrochloric acid at a pH of about 0.8 but by the it is mixed with the stomach contents.

A

gastric glands

71
Q

these enzymes are capable of digesting

A

° protein
° collagen
° nucleoprotein into proteoses, peptones and polypeptides

72
Q

Digestion of proteins in the intestine

A
  1. Digestion of protein by pancreatic secretions
  2. Digestion of polypeptides by the epithelial enzymes of the small intestine
73
Q

when the proteins leave the stomach, they ordinarily are in the forms of proteoses, peptones, large polypeptides and amino acids.

A

Digestion of proteins by pancreatic secretions

74
Q

two sourcea pf protein are available for the ruminant to use.

A

protein from feed and microbial protein from microbes that inhabit its rumen

75
Q

unique in that it has a symbiotic relationship with these microbes.

A

ruminant

76
Q

rumen bypass protein

A

undegradable intake protein (UIP)

77
Q

are used by the microbes along with the energy from carbohydrate digestion for growth and reproduction

A

rumen microbes breakdown the DIP into ammonia (NH3), amino acids and peptides.

78
Q

the ammonia in rumen liquor is the key intermediate in the microbial degradation and synthesis of protein

A

ammonia production

79
Q

comes from overfeeding urea to ruminants

A

urea toxicity

80
Q

rumen microbes for their rapid multiplication utilize considerable protein and utilize and fix it as excellent body protein composing of essential.

A

fate of ammonia

81
Q

it is now well established that blood urea enters back into the rumen directly by transfusion through rumen wall and also indirectly through saliva

A

urea recycling

82
Q

microbes in the rumen degrade large proportion of dietary proteins and utilize some of the degradation products for their own protein synthesis.

A

microbial protein synthesis

83
Q

ruminants can utilize non-protein nitrogenous compound as a source of protein through the microorganisms.

A

utilization of non-protein nitrogen compound

84
Q

white crystalline, deliquescent solid

A

urea

85
Q

also used as ruminants feed

A

feces

86
Q

nervousness, muscle tremors, difficulty in respiration, excessive salivation, bloat, tetany, convulsions and death within 2 to 3 hrs are the symptoms of urea toxicity.

A

urea toxicity symptoms

87
Q

also able to utilize NPN compound for the synthesis of non-essential amino acids and optimum level is 0.3 % of the diet.

A

utilization of NPN substance by non-ruminants

88
Q

the absorbed amino acids in the body are utilized for various functions

A

utilization of amino acids

89
Q

4 utilization of amino acids

A
  1. for the protein synthesis
  2. for the synthesis of essential amino acids
  3. as a source of energy and ammonia
  4. for a special function
90
Q

proteins are synthesized from amino acids, which become available as the end products of digestion or as the result of synthetic process within the body

A

protein synthesis

91
Q

four stages of process of protein synthesis

A

1) activation of individual amino acids
2) initiation of peptide chain formation
3) chain elongation
4) chain termination

ZOOTH 212 (Animal Nutrition) (4 decks)

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