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Ruminant Nutrition > Protein Study > Flashcards

Protein Study Flashcards

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1
Q

what are proteins?

A

essential components of animal tissue

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2
Q

chemically, amino acids consists of?

A

alpha carbons
amino groups
carboxyl group
side chains

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3
Q

how many AA are there

A

300

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4
Q

how many AA used for protein synthesis

A

20

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5
Q

2 isomeric forms AA can exists

A

D and L isomers

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6
Q

key points of L-isomer

A

only one used in proteins
used nationally
D made into L to make protein

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7
Q

proteins are macromolecules of?

A

amino acid chain

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8
Q

Amino acids classified based on

A

Structure
Essentiality
Polarity
Electrical Charge

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9
Q

what is important about each characteristics

A 
structure = distinct side chain
Essentiality = dietary requirements 
Polartiy = non-polar v polar
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10
Q

Structure and Essentiality similarities

A

side chain determines if AA are synthesized by mammalian cells

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11
Q

Polarity

A

when AA interact with water at physical pH

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12
Q

electrical charge

A

charge of amino acid in aqueous solution at physical pH

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13
Q

what synthesizes amino acids

A

microbes

diet (plants)

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14
Q

what doesn’t synthesizes amino acids

A

animals

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15
Q

amino acids essential and non-polar

A 
valine
methionine
leucine
tryptophan
isoleucine
phenylalanine
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16
Q

amino acids nonessential and nonpolar

A

glycine
alanine
proline

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17
Q

amino acids essential and polar

A

arginine
histidine
lysine
theronine

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18
Q

amino acids nonessential and polar

A 
tyrosine
cysteine
serine
aspartate
asparagine
glutamate
glutamine
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19
Q

amino acids that are branched

A

valine
leucine
isoleucine

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20
Q

sulfur containing amino acids

A

methionine

cysteine

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21
Q

amino acids considered aromatic

A

trytophan

phenylalanine

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22
Q

which amino acids transport nitrogen

A

aspartate

glutamate

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23
Q

what amino acid in pigs and chicken with corn

A

Lysine

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24
Q

amino acids not branched

A

Theronine

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25
what is wrong with Proline?
digestive issues due to Nitrogen side chain
26
what are essential amino acids?
required in diet and mammalian cells can't synthesize proper amounts
27
what are limiting amino acids?
EAA that are limited in diet
28
what are non-essential amino acids?
not required in diet due to mammalian cells making sufficient amounts
29
why is arginine considered semi-essential?
can be synthesized in body NOT in proper amounts
30
limiting amino acids in ruminants
Methionine
31
limiting amino acids in pigs
Lysine
32
what are protein chains made of?
amino acids
33
amino acids linked by?
peptide bonds
34
what are dipeptides?
2 amino acids linked
35
what are polypeptides?
greater than 10 amino acids linked
36
what are protein synthesis based on
genetic code
37
what's transcription?
DNA code copied to mRNA
38
what's translation?
mRNA used to assemble an amino avid chain
39
what biological properties of protein does genetic code determine
AA protein contain AA sequence length of AA chain spatial relationship of AA within protein
40
what protein is made with high levels of cystine
keratin | ex. hair
41
4 levels of structural organization in proteins
Primary Secondary Tertiary Quartenary
42
what does the primary structure consists of
sequence of amino acids linked by peptide bonds
43
what does secondary structure consists of
coiling of folding polypeptide chains to alpha-helix/beta-pleated sheets from H bonds
44
what does the tertiary structure consists of
3-D folding of chain by H bonds and electrostatic attractions
45
what does the quartenary structure consists of
protein macromolecules formed by polypeptide chains by H bonds and electrostatic attraction
46
how are proteins classified
based on composition, solubility, nutritive value, shape, size and function
47
microbes provide how much protein for ruminants
50 - 80%
48
what is the ultimate goal of protein digestion?
- pieces of food converted to smaller digestible portions | - hydrolysis of peptide bonds to produce free AA
49
what does digestive enzymes do?
break peptide bonds
50
name of digestive enzymes secreted as inactive pro-enzymes
zymogens
51
what is exopeptidases?
cleave amino acids at terminal end of protein molecules
52
what is endopeptidases?
hydrolyse peptide bonds within primary protein structure
53
Characteristics of HCl in protein digestion
- released from parietal cells - pH = 1.6 - 3.2 - Denatures 4, 3 and 2 structures
54
Characteristics of Pepsiogen in protein digestion
- released from chief cells | - works with HCl to become pepsin
55
Characteristics of Pepsin in digestion
- Endopeptidase | - cleaves side of amino side of aromatic AA
56
active form? | inactive form?
``` active = pepsin inactive = pepsinogen ```
57
pH of small intestine in non-ruminant protein digestion
7 - 8
58
pancreatic enzymes secreted in small intestine of non-ruminant
``` Trypsinogen Chymotrypsinogen Procarboxypeptidase Proelastase Collagenase ```
59
Intestinal brush border enzymes secreted
Aminopeptidases | Dipeptidases
60
Trypsinogen activated by and converted to
``` Activated = Enteropeptidase Converts = Trypsin ```
61
Chymotrypsinogen activated by and converted to
Activated = Trypsin | Converted --> Chymotrypsin
62
Procarboxypeptidase activated by and converted to
Activated = Trypsin | Converted --> Carboxypeptidase
63
where does aminopeptidase cleave
Nitrogen terminal of AA
64
dipeptidases cleave what?
dipeptides
65
what are proteins broken down to?
- Tripeptides - Dipeptides - Free AA
66
Characteristics of Trypsin inhibitors?
- small proteins & peptides - inactivated by heat - block digestion of proteins - found in plants, organs and fluids
67
Ruminally Degradable Proteins
proteins available to the rumen microbes
68
Ruminally Undegradable Protein
protein that escapes rumen fermentation and goes to small intestine
69
Non Protein Nitrogen
not true protein providesa source of Nitrogen
70
Microbes break down dietary proteis
- amino acids - NH3 - VFAs - CO2
71
Factors that affect ruminal degredation
- Heat Treatment - Rate of Passage - N and S availability - Energy availability

Ruminant Nutrition (5 decks)

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