Protein Flashcards
which amino acid is high in sulfur
methionine
MATT amino acids
Methionine
Arginine
Threonine
Tryptophan
HILL amino acids
Histidine
Isoleucine
Leucine
Lysine
VP amino acids
Valine
Phenylamine
T/F essential amino acids are synthesized by the body
FALSE, they must be fed in the diet at the required levels
which animals are fed at their amino acid level(fed exactly the amount they need)
Pigs
chicken
Can ruminal microbes synthesize essential amino acids, if so how?
yes, they can synthesize all amino acids from ammonia and carbon skeleton
what type of ruminant(job) exceeds the microbes AA production abilities
-High-producing dairy cow
-Implanted, high growth steer grazing wheat pasture
what AA is used for milk production
methionine
T/F ALL proteins contain ALL AA in some amount
TRUE
maintenance AA requirements definition
AA needed to stay alive
factors increasing protein requirements
Increased:
Size
growth
lactation
gestation(last 1/3)
gender(male>female)
weight
activity
certain genetics
sick
polypeptide AA amount
> 10 AA
Tripeptide, dipeptide AA and peptide bond amount
Tri- 3 AA, 2 peptide bonds
Di- 2 AA, 1 peptide bond
levels of protein structure
Primary(1°)- Sequence of AA
Secondary(2°)- hydrogen bonding
Tertiary(3°)-clustering of hydrophobic regions
Quaternary(4°)-interaction of polypeptides
what levels of protein can be broken down by HCl
2,3,4
T/F Proteolytic enzymes(pepsin) are required to break peptide bonds(1°)
TRUE
steps of protein digestion
-denaturing(HCL: stomach)
-hydrolysis of peptide bonds(mammalian & proteolytic enzymes: stomach and SI)
-absorption(AA, di, tri)
pepsinogen:
-production site
-activator(s)
-enzyme name
-site of activity
-activity
-stomach
-HCL/Pepsin
-pepsin
-Stomach
-endopeptidase
Trypsinogen:
-production site
-activator(s)
-enzyme name
-site of activity
-activity
-pancreas
-endopeptidase trypsin
-trypsin
-SI
-endopeptidase
Chymotrypsinogen:
-production site
-activator(s)
-enzyme name
-site of activity
-activity
-pancreas
-trypsin
-chymotrypsin
-SI
-endopeptidase
Procarboxypeptidase:
-production site
-activator(s)
-enzyme name
-site of activity
-activity
-pancreas
-trypsin
-carboxy peptidase A&B
-SI
-exopeptidase
endopeptidase define
hydrolyze peptide bonds on interior of peptide
exopeptidase define
hydrolyze peptide bonds on end of peptide
enteropeptidase(enterokinase) define
produced by enterocytes in response to CCK and secretin(activate trypsin)
what activates I and S cells
presence of low pH digesta(they detect low pH)
brush border peptidase
amino peptidase
dipeptidyl amino peptidase
tripeptidase
function of amino peptidase
cleave 1 AA from oligopeptides
function of dipeptidyl amino peptidase
cleave 2 AA from oligopeptides
function of tripeptidase
cleave specific AA from tripeptides
what causes a decrease in zymogen production
excess free trypsin
Ruminant undegradable protein(RUP/UIP)
-undegradable by microbes
-80% digestible by animal(average)
ruminally degradable protein(RDP/DIP)
-degradable by microbes(100% digestible)
-used by microbes to synthesize MCP
T/F and Kp increases, RDP decreases and RUP increases
TRUE
nitrogen retention at maintenance
0
nitrogen retention during growth
> 0
growth phase attributes
PS>PD, both increase
muscle loss phase attributes
PS<PD, both decrease
nitrogen retention during muscle loss
<0
what factors influence MCP production
-supply of fermentable organic mater(glucose)
-supply of RDP
T/F microbes will improve quality of low-quality RDP and lower quality of high quality RDP
TRUE
