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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
amino acids which are never found as constituents of proteins but which either play metabolic roles occur as natural products.
non protein amino acids
26
amino acid which is present in a protein in the least amount in relation to be animal's need.
limiting amino acid
27
livestock in definite proportions requires the essential amino acids.
limiting amino acid
28
the limiting amino acid of corn
lysine
29
can be considered under four basic heading: primary structure, secondary structure, tertiary structure and quaternary structure.
Structure of proteins
30
4 Structure of Proteins
1. Primary structure 2. Secondary structure 3. Tertiary structure 4. Quaternary structure
31
structure that proteins are built up from amino acids means of a linkage between the a-carboxyl of one amino acid
primary structure
32
refers to the sequence of amino acid along the polypeptide chains of protein.
primary structure
33
structure that peptide chain exist in the form of a right-handed-helix.
secondary structure
34
structure which describes how the chains of the secondary structure further interact through the R-groups of amino acid residues.
Tertiary structure
35
structure that contain more than one polypeptide chain
quaternary structure
36
what are the classification of proteins?
I. Fibrous Proteins II. Globular Proteins III. Conjugated Proteins IV. Derived Proteins
37
these proteins are insoluble and very resistant to animal digestive enzymes
fibrous proteins
38
3 types of fibrous proteins
a. collagens b. elastin c. keratins
39
main proteins of connective tissues.
collagens
40
protein found in elastic tissues such as tendon and arteries.
elastin
41
protein of hair, hoof, nails etc.
keratins
42
important component of collagens
hydroxyproline
43
contain about 4 percent sulphur
wool protein
44
this group includes all the enzymes, antigens and hormones that are protein.
Globular Proteins
45
4 Globular Proteins
a. albumin b. globulins c. histones d. protamines
46
water-soluble and heat coagulable and occurs in eggs, milk, blood and many plants.
albumin
47
present in eggs, milk and blood and are the main reserve protein source in seed.
globulins
48
are basic protein, which occur in cell nucleus where they are associated with DNA.
Histones
49
are basic protein of relatively low molecular weight, which are associated with nucleic acid.
protamines
50
are composed of simple protein combined with some nom-protein substances as prosthetic group.
conjugated proteins
51
4 conjugated proteins
a. phosphoprotein b. glycoprotein c. lipoprotein d. chromoprotein e. nucleoprotein f. metalloproteins
52
protein' which on hydrolysis yields phosphoric acid and amino acids.
phosphoprotein
53
casein of milk and phosvitin of egg yolk
phosphoproteins
54
conjugated proteins with one or more heterosaccharides as prosthetic groups.
glycoproteins
55
proteins conjugated with lipid lecithin and cholesterol
lipoproteins
56
contain pigment as a prosthetic group.
chromoprotein
57
are compound of high molecular weight and conjugated with nucleic acid
nucleoproteins
58
a large group of enzyme proteins comtain metallic elements, such as Fe, Co, Mn, Zn, Cu, Mg, etc.
metalloproteins
59
this class of proteins includes those substances formed from simple and conjugated proteins.
derived proteins
60
2 derived proteins
1. Primary derived proteins 2. Secondary derived proteins
61
not classed as proteins occur in plants and animals
non-protein nitrogenous compounds
62
high molecular weight compounds which, on hydrolysis yield a mixture of basic nitrogenous compound a pentose and phosphoric acid
nucleic acid
63
they are carbohydrates derivatives in which purines and pyrimidines found in the nucleic acids.
Nucleosides and nucleotides
64
AMP stands for?
adenosine monophosphate
65
ADP stands for?
adenosine diphosphate
66
ATP stands for?
adenosine triphosphate
67
softens the food particles, which is helpful for ingestion of protein.
saliva
68
there is no digestion of protein in the mouth because saliva has no proteolytic enzyme
Digestion of Protein in Non-ruminants
69
are the most important peptic enzymes of the stomach.
pepsi and gastricin
70
secrete hydrochloric acid at a pH of about 0.8 but by the it is mixed with the stomach contents.
gastric glands
71
these enzymes are capable of digesting
° protein ° collagen ° nucleoprotein into proteoses, peptones and polypeptides
72
Digestion of proteins in the intestine
1. Digestion of protein by pancreatic secretions 2. Digestion of polypeptides by the epithelial enzymes of the small intestine
73
when the proteins leave the stomach, they ordinarily are in the forms of proteoses, peptones, large polypeptides and amino acids.
Digestion of proteins by pancreatic secretions
74
two sourcea pf protein are available for the ruminant to use.
protein from feed and microbial protein from microbes that inhabit its rumen
75
unique in that it has a symbiotic relationship with these microbes.
ruminant
76
rumen bypass protein
undegradable intake protein (UIP)
77
are used by the microbes along with the energy from carbohydrate digestion for growth and reproduction
rumen microbes breakdown the DIP into ammonia (NH3), amino acids and peptides.
78
the ammonia in rumen liquor is the key intermediate in the microbial degradation and synthesis of protein
ammonia production
79
comes from overfeeding urea to ruminants
urea toxicity
80
rumen microbes for their rapid multiplication utilize considerable protein and utilize and fix it as excellent body protein composing of essential.
fate of ammonia
81
it is now well established that blood urea enters back into the rumen directly by transfusion through rumen wall and also indirectly through saliva
urea recycling
82
microbes in the rumen degrade large proportion of dietary proteins and utilize some of the degradation products for their own protein synthesis.
microbial protein synthesis
83
ruminants can utilize non-protein nitrogenous compound as a source of protein through the microorganisms.
utilization of non-protein nitrogen compound
84
white crystalline, deliquescent solid
urea
85
also used as ruminants feed
feces
86
nervousness, muscle tremors, difficulty in respiration, excessive salivation, bloat, tetany, convulsions and death within 2 to 3 hrs are the symptoms of urea toxicity.
urea toxicity symptoms
87
also able to utilize NPN compound for the synthesis of non-essential amino acids and optimum level is 0.3 % of the diet.
utilization of NPN substance by non-ruminants
88
the absorbed amino acids in the body are utilized for various functions
utilization of amino acids
89
4 utilization of amino acids
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
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
protein synthesis
91
four stages of process of protein synthesis
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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