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Nutrition > Proteins > Flashcards

Proteins Flashcards

1
Q

The word protein was derived from the Greek word ——- which means the —— (——– —— ———)

A

proteios; first (the most important).

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2
Q

Proteins are organic nutrients; highest concentration in —— —— of animals.

A

muscle tissues

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3
Q

Proteins are Expressed in terms of —— ——

A

crude protein (CP).

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4
Q

CP = ———- + — ——- ——

A

CP = true protein + non-protein nitrogen (NPN

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5
Q

Formula for Crude Protein

A

CP = %N × 6.25%

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6
Q

are proteins which are composed of amino acids only.

A

True proteins

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7
Q

—— ——- —–are compounds which are not true protein in nature but contain nitrogen (N) that can be converted to protein by ——– ——.

A

Non-Protein-Nitrogen; bacterial action.

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8
Q

Normally, —— animals receive a diet higher in protein content than
——- and ——— animals.

A

young; growing and mature

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9
Q

Young animals require high amount of amino acids to

A

support growth of tissues.

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10
Q

Mature animals need amino acids largely for

A

maintenance of protein tissues.

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11
Q

Proteins are large molecules with molecular weights ranging from —– to —- ——–.

A

5000 to many millions.

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12
Q

Proteins are chemically made up of

A

C (50-55%), H (5-8%), O (20-25%), N
(15-17%), S (1-3%) and P (0.20-1.5%).

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13
Q

Proteins are made up of molecules of —— —— which are linked
together by —— ——-

A

amino acids; peptide bonds

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14
Q

The amino acids are organic compounds that contain

A

one or more amino group (NH2).

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15
Q

Proteins contain —- —- – amino acids; polypeptides contain —- —- – amino acids.

A

more than 70; less than
70

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16
Q

ontains only amino group and lacks the carboxylic acid group
as compared to amino acid structure

A

Non-Protein-Nitrogen Source

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17
Q

NPN with 1 N -
NPN with 2 N -
NPN with 3 N -

A

Ammonia
Urea
Biurey

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18
Q

have a fiber structure and are insoluble in water; serve predominantly as supporting and ground substances. Ex. —— in hair; —— and —– in connective tissue.

A

Scleroprotein

Keratin; collagens and elastins

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19
Q

are more or less strongly coiled and are soluble in water and salt solutions. Ex. —— in the nucleus, albumins and
globulins

A

Spheroproteins

Histones

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20
Q

contain amino acids which can be
split-off relatively easy

A

Conjugated Proteins or Proteids

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21
Q

in hemoglobin;
in casein;
in serum liprotein,
in nucleic acid;
in seromucoid and
in myoglobulin).

A

Metalloprotein
phosphoproteins
lipoprotein
nucleoprotein
glycoprotein
chromoprotein

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22
Q

proteins that yield only amino acids or their derivatives upon hydrolysis.

A

Simple Proteins

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23
Q

these are proteins conjugated with a non-protein radical (prosthetic group).

A

Conjugated Proteins

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24
Q

• – conjugated to nucleic acid (DNA and RNA)
• – with phosphate (casein of milk)
• – contains a metal ion cofactor (cytochrome oxidase)

A

Nucleoproteins
Phosphoproteins
Metalloprotein

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25
Q

• – conjugated to lipid (very low density lipoprotein)
• – contain a nucleic acid derivative of riboflavin (flavin-adenine
dinucleotide or FAD)
• – contain oligosaccharide chains (immunoglobulins)

A

Lipoprotein
Flavoprotein
Glycoprotein

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26
Q

contain one amino acid and one carboxyl group

A

Neutral amino acids

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27
Q

3 types of Neutral Amino Acid

A

Aliphatic Amino Acids
Aromatic Containing Compounds
Sulfur Containing Compounds

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28
Q

Aliphatic amino acids (7)

A

glycine, alanine, valine, leucine, isoleucine, serine and threonine

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29
Q

Aromatic amino acids (3)

A

phenylalanine, tyrosine, tryptophan

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30
Q

Sulfur containing amino acids (3)

A

cystine, cysteine, methionine

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31
Q

have an excess of carboxyl over amino groups

A

Acidic amino acids

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32
Q

Acidic Amino Acid (2)

A

Aspartic Acid and Glutamic Acid

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33
Q

– possess an excess of basic groups

A

Basic Amino Acids

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34
Q

3 Basic Amino Acids

A

Histidine Arginine and Lysine

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35
Q

have imine functional group

A

Imino acids

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36
Q

2 Imino Acids

A

Proline and Hydroxyproline

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37
Q

• amino acids which are essential to the animal

• must be supplied to the diet because the animal’s body cannot synthesize
them fast enough to meet needs for these amino acids.

A

Essential Amino Acids (EAA)/Indispensable Amino Acids (IAA)

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38
Q

makes up 40% of tissue protein

• amino acids which are needed by animals but can be synthesized by them in amounts sufficient for their needs.

A

Non Essential Amino Acids/Dispensable Amino Acid

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39
Q

with — —– – ——, tissue synthesis of —– occur provided that there is adequate supply of amino nitrogen and source of carbon and energy.

A

With Low intake of Non Essential Amino Acids

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40
Q

Amino acid which is present in a protein in the least amount in
relation to the animal’s need for that particular amino acid

A

Limiting Amino Acid

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41
Q

first limiting amino acid of corn-soy diets in growing pigs

A

Lysine

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42
Q

common limiting amino acids in
poultry diets especially in corn-soy diets

A

Methionine and cystine

43
Q

A protein of high quality contains the —– in amount and relationship
corresponding to the requirement of the animal.

A

Essential Amino Acids

44
Q

——– protein sources (e.g. fish meal and skimmilk) are generally
superior in protein quality than —– protein sources (e.g. soybean
meal; ipil-ipil leaf meal).

A

Animal; plant

45
Q

Denaturation of proteins by the ——— —— secreted by the stomach (proventriculus in poultry) leading to the change in the native
structure of protein

A

hydrochloric acid (HCl)

46
Q

Digestion of denatured protein digestion at — – (–) through the
action of enzyme —– that results to the formation of large peptides
and amino acids

A

Low ph 2.1; pepsin

47
Q

Translocation of peptides and amino acids to the —– —— and
which they are acted upon further by specific enzymes: ——-, ——–, ——-, ———-, ——-, ——–

A

Small intestine; chymotrypsin, carboxypeptidase, aminopeptidase, nucleotidase and
nucleosidase

48
Q

are absorbed and transported to the liver via portal circulation where they are metabolized.

A

freed amino acids

49
Q

Factors Affecting Protein Digestion by Non-Ruminants

A
  1. Age of Animal
  2. Presence of Protease Inhibitors
  3. Excessive heat processing of feeds
50
Q

low protein digestibility during the first —— —— due to
limited amount of digestive enzymes; digestibility increases within this
period (- to - —–) then not much change after.

A

Age of Animal; Four weeks (1 to 4 weeks)

51
Q

——- ——- in raw soybeans,
—– —– in rice bran,
—— in peas,
in by-product feeds and
in cereals (e.g. barley and wheat) and ——– (soybean);

these inhibitors limit the activity of enzymes for protein digestion.

A

Trypsin Inhibitor
Phytic acid
lectins
fiber
non-starch polysaccharides (NSP)
legumes

Presence of Protease Inhibitors

52
Q

Excessive heat processing of feeds – cause ——-/——- reaction that
leads to the binding of amino acids such as lysine with glucose or lactose
rendering them biologically unavailable.

A

Maillard/Browning

53
Q

The rumen organisms are capable of utilizing almost any nitrogen
source to create ———- (serves to provide protein needs of
the ruminant animal) and thus enable the ruminant animal to use
——- which are unsuitable for use by non-ruminant animal

A

bacterial protein; feedstuffs

54
Q

About what percent of the true protein escapes microbial action in the rumen??

What do you call about the protein that escapes microbial action in the rumen that passes into the abomasum and small intestine where it is absorbed and digested in the same
manner as in the non-ruminant?

A

40% ; escape protein or by-pass protein

55
Q

The dietary NPN and the remaining portion of the true protein (about
—%) are acted upon by the —– ——- forming ammonia (NH3).

A

60%, rumen microflora

56
Q

With adequate amounts of fermentable carbohydrates, the —-
is used by the rumen bacterial to form bacterial protein.

A

NH3 (Ammonia)

57
Q

The bacterial protein then passed into the ———– and digested as
previously presented for non-ruminants

A

abomasum

58
Q

The ——- —— which is formed may be of better or poorer quality
than that of the ingested feed

A

microbial protein

59
Q

Usually, the quality of protein from moderate to poor diets may be
improved by —– ——- while the quality of protein of good to high
quality protein may actually be ——.

A

Rumen metabolism; reduced

60
Q

—% of the bacterial species in the rumen utilize nitrogen solely for growth, —-% have absolute requirement for nitrogen, —- use either ammonia
(NH3) or amino acids.

A

80%, 26%, 55%

61
Q

cannot utilize NH3; they consume bacteria as a source of nitrogen and also from particulate matter.

A

Protozoa

62
Q

Unused quantity (by rumen microbes) of NH3 are transported to the
—- and converted into —-.

A

Liver; Urea

63
Q

Urea is either excreted by the —— through the urine or recycled
into the rumen by way of the —–.

A

Kidney; saliva

64
Q

If the amount of NH3 which enters the bloodstream is excessive and
exceeds the ability of the animal to excrete it, it can lead to ——- and —–.

A

toxicity and death.

65
Q

Factors Affecting Protein Digestion by Ruminants

Availability of ——– ——-
Quantity of —- ——- and —- (specific need of the rumen microflora)
• —– —— (related to quantity of fermentable carbohydrates)
• Degradability of the —–
• —— population

A

fermentable carbohydrates
true protein and NPN
Dietary energy
protein
Microbial

66
Q

Fates of Absorbed Amino Acids

    • new and replacement of worn out
      tissues.
      • Collagen
      • Elastin
      • Contractile proteins
      • Ketratin
      • Blood protein
  2. Used in —- ——-
    • Enzymes – digestion, anabolism and
    catabolism
    • Hormones
    • Immune bodies
  3. – release of
    amino group from the carbon
    skeleton and entry of the
    carbon skeleton to the Kreb’s
    Cycle.
A
  1. Use as a basic structural unit of the Animal
  2. Used in body metabolism
  3. Source of energy after
    deamination
67
Q

the key organ in nitrogen metabolism

A

Liver

68
Q

Functions of Liver
• —– ——
• Supply of —– —– to the ——– when needed
• Processes ——– for ——– when in excess

A

Protein synthesis

Supply of amino acids to the circulation when needed
Processes nitrogen for excretion wgen in excess

69
Q

occurs in the mitochondria;

A

Transamination

70
Q

permits exchange of ammonia from an amino acid to the keto moiety of an alpha-keto acid.

A

Transamination

71
Q

Transamination promotes the following events:
a. Excess amino acid can be relieved of their NH3 and the keto acid
metabolized in the TCA cycle for ——-
b. Synthesis of —- from glutamic acid and TCA intermediates.

A

Energy generation; NEAA

72
Q

are the most important enzymes for transamination.

A

Glutamic acid transaminase and alpha ketoglutaric acid transaminase

73
Q

• Of the EAA, only —– and ——– do not participate in transamination.

A

lysine and threonine

74
Q

Transamination is a ——- process and requires —— as a cofactor

A

Reversible; vitamin B6

75
Q

is the removal of amino group from amino acids.

A

Deamination

76
Q

Two types of Deamination

A

Oxidative and Non-Oxidative

77
Q

it occurs in the cytosol and mitochondria of most cells.

A

Oxidative

78
Q

the principal enzyme involved in the process of deamination is - - ——— ———–.

A

L-glutamate dehydrogenase.

79
Q

NH4 enters —- Cycle and alpha-ketoglutarate enters — Cycle

A

Urea cycle and TCA Cycle

80
Q

catalyze by amino acid dehydratase and requires vitamin B6

A

Non-Oxidative

81
Q

is the principal activity of the cell.

A

Synthesis of protein

82
Q

is the template of protein synthesis thru transcription followed by Translation.

A

DNA

83
Q

(copying a segment of DNA to mRNA)

A

Transcription

84
Q

(translating the sequence of mRNA to a sequence of amino acids)

A

Translation

85
Q

Three RNAs are involved in the process, namely

A

mRNA
rRNA
tRNA

86
Q

determines sequence of amino acids in the protein being formed;

A

Messenger RNA (mRNA)

87
Q

constitutes 2/3 of the mass of ribosome, part of the structure of ribosome which is the site of protein synthesis.

A

Ribosomal RNA (rRNA)

88
Q

smallest of the RNAs; carries specific amino acid to be
incorporated in the polypeptide chain;

A

Transfer RNA (tRNA)

89
Q

there are – separate tRNA – –
attuned to specific amino acid; - signals peptide chain termination.

A

64; 61; 3

90
Q

requirement can be met only by providing adequate
levels of methionine in the diet.

A

Methionine

91
Q

requirement can be met by methionine + serine

A

Cystine

92
Q

requirement can be met only by phenylalanine

A

Phenylalanine

93
Q

requirement can be met by phenylalanine

A

Tyrosine

94
Q

– can be used interchangeably

A

Glycine and Serine

95
Q

Advantages of Expressing Amino Acid Needs Based on Digestible Amino Acids

  1. Improves —— and —— of feed manufacturing.
  2. Real — —- —- ——- can be obtained.
  3. —— —— —– is more indicative of the relative nutritional
    value of feedstuffs. Allows use of protein feeds of poor quality at
    high levels.
  4. ——– ——- of protein/amino acids.
A

accuracy and precision
low-cost feed formula
Digestible amino acid
Minimize wastage

96
Q

high dietary level may compensate for a deficiency of choline or vitamin B12 by providing methyl group.

A

Methionine

97
Q

alleviates niacin deficiency through metabolic conversion to niacin.

A

Tryptophan

98
Q

most metabolic activities are depressed with —– ——–;
there are no specific set of deficiency signs for protein.

A

Protein deficiency

99
Q

With low protein intake the following can be observed:

b. Growth is ——– (as in the case of ——– which is
protein malnutrition in young humans)
c.
d.

A

rumen fermentation
impaired; Kwashiorkor
Sub-optimal reproduction
d. Sub-optimal lactation and reproductiob

100
Q

a deficiency of any of the essential amino acids is in effect a protein
deficiency.
• an amino acid deficient diet causes prompt ——- in —– ——
of an animal.

A

Amino acid Deficiency;

reduction in feed intake

101
Q

this results from the addition to a low protein diet of one or more
amino acids, other than the growth limiting one, in amounts that are
not individually toxic and yet causes depression in food intake and
growth that are readily prevented by a supplement of the —— ——– —– —-

A

Amino acid imbalance
growth-
limiting amino acid.

102
Q

it is a condition wherein one amino acid affects the requirement of
another by interfering with its metabolism.

A

Amino acid Antagonism

103
Q

Example of Amino Acid antagonism

A

Lysine-arginine antagonism

104
Q

——- (given at high level) increases the requirement for arginine
by competing with arginine for reabsorption in the —– ——
increasing arginine excretion and by increasing renal arginase
activity and thus splitting arginine into —– and ——–.

A

Lysine
renal tubules
urea and ornithine

Nutrition (6 decks)

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