Flashcards Animal Nutrition Exam 4/ Quiz 4 Material

skeletal muscle, connective tissues, protective protein

what are the 3 main functions of proteins

kjeldhal

what allows us to measure the Nitorgen content in proteins

the nitrogen wihtin protein

when we are talking about crude protein what does that actually talk about

hydrogen, amino group, carboxyl group, r- group that changes for each AA

what are the four groups attatched to the central carbon of a protein

phenylalanine, valine, threonine, tryptophan, isoleucine, methionine, histodine, arginine, leucine, lysine

what are the 10 "essential amino acids"

Classified nonessential vs. essential AAs. 1930, University of Illinois, a growing rat

what did Dr. rose do? when? where? what was his model?

only required during growth (we believe it is not required after puberty, we now think its required by dam during pregnancy)

in terms of being essential, explain the exception for arginine

chickens/turkers/ other avians require it for feathers and uric acid production

in terms of being essential, explain the exception of glycine

an imino acid that is essential for cats

in terms of being essential explain taurine

covalent bonds linking AA together: dipeptide (2 AA), peptide (3-8 AA), Polypeptide (more 8-10 AA)

what are peptides and what are the 3 classes

the AA it is made of

the function of a protein is dependent on what

important for maintaining protein structure

what is the function of disulfide bonds

the terminal AA

glycine is what part of a protein

AA within the protein

cysteine is what part of an protein

AA sequence of the protein

the primary protein holds what function

involves bonding with disulfide bonds

the secondary protein holds what function

3D shape caused by hydrophilic and hydrophobic AAs

tertiary proteins hold what function

neutral and aromatic AAs that go inside the protein structure

explain hydrophobic AA

acid and base AA that go on the outside of the protein structure

explain hydrophilic AA

Irreversibly unfold a protein to decrease 3D structure, which decreases activity. Heat, chemically, decreasing pH with HCl

what does it mean to denature a protein? what methods are used to do this?

Break down protein to AA for absorption

what is the goal of monogastric digestion?

HCl from parietal cells will decrease pH, which causes proteins to denature and activates pepsinogen to become pepsin. Pepsinogen from the cheif cells acts as a proteolytic enzymes/ endopeptidase that cleaves peptide bond somewhere in the middle of the sequence

what happens in the mongastric stomach in terms of protein digestion - explain what enzymes are used.

trypsin and chymotrypsin are endopeptidases and carboxypeptidase is an exopeptidase

what are the pancreatic enzymes used in a mongastric duodenum for protein digestion

mucosal cells such as enterokinase, aminopeptidase, and dipeptidase

what are the duodenal enzymes used in monogastric duodenum for protein digestion

enterokinase

what activates trypsin in the duodenum of a mongrastic during protein digestion

1. transcirption of DNA to RNA

2. mRNA is read, and a codon of 3 AAs is made

3. tRNA carries specific AA to ribsome pro protein sythesis and recognizes codons on mRNA

mRNA + tRNA-AA1 + tRNA-AA2 + tRNA-AA3 = AA1- AA2-AA3

explain the process of protein sythesis

constant protein turnover that is energy demanding (4 ATP) tht ispart of the maintenance req

explain turnover

deficiency of one essential AA stops the entire process of synthesis. The first AA that runs out is known as the first limiting AA. this also depends on the animals diet

explain limiting AA concept

constant turnover. 75% is reused for protein synthesis and 25% catabolized. if we run out of an AA and sythesis stops then the rest of the AA are catbolized. can also occur if there is too much of an AA. used to make energy

explain catabolism

- deamination: removing the amino group as ammonia

- transamination: trasnfer of amino group from a AA to a ketoid

what are the 2 types of catbolic reactions and their functions

AA --enzyme, H2O--> keto acid + ammonia

what is the reaction for deamination

1 AA + 2 KA <-- enzyme, vitamin B6(pyroxidine) --> KA 1 + AA 2

what is the reaction for transammination

leucine and isoleucine. make acetyl coa

in reference to ketogenic AA, what are they and what do they make

all other AA except fot leucine and isoleucine

in reference to glutoneogenic AA, what are they

pyruvate

what amino acid is commonly used in glycolysis

oxaleoacetate, a- ketoglutarate, aceytl coa, succinycholine coa, fumarate

what amino acids are used in krebs cycle

muscle tremors, slurred speech, blurred vision, ataxia, tetany

what are the common symptoms of ammonia toxicity

when the removal of amine groups during amino acid breakdown (deamination) outpaces the liver's ability to convert the resulting ammonia into safe urea

how does ammonia toxicity occur

3 ATP from 4 high-energy phosphate bonds. the cycle will remove/ detoxify the ammonia created from deamination

In reference to the urea cycle, how many ATP are needed? what is the role of the cycle?

Urine for monos. saliva for rums, avians will isntead make uric acid

where can BUN escape to in mongastrics? ruminants? birds?

glycine. uric is used as an excretory product

what are the requirments for making uric acids in birds?

secrete protease that breaks protein down into AA and also deaminate AA to relase ammonia, carbon skeletons, ketoacids

what is the function of bacteria in ruminent protein digestion

protein sythesized by microbes themselves when they resuse those deminated AA to make new AA

explain microbial proteins

none

what are the essential AA for ruminants

non protein nitrogen (NPN) and true protein

what are the 2 sources of protein in a ruminent animal

proteins that do not undergo ruminal degradation

explain escape protein

microbial protein and escape protein

what 2 proteins are actually digested by ruminants

phenylalanine, valine, threonine, tryptophan, isoleucine, methionine, histodine, arginine, leucine, lysine

according to the dietary requirment method, what are the 10 essential AAs

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

what are the 7 neutral AAs

Aspartic acid transforms to asparagine andglutamic acid transforms to glutamine

what are the 4 acidic AAs

histadine, arginine, lysine

what are the 3 basic AAs

phenylalanine, tyrosine, tryptophan

what are the 3 aromatic AAs

cystine, cytseine, methionine

what are the 3 sulfuric AAs

neutral

what classification is this AA

neutral

what classification is this AA

neutral

what classification is this AA

neutral

what classification is this AA

neutral

what classification is this AA

neutral

what classification is this AA

neutral

what classification is this AA

acidic

what classification is this AA

acidic

what classification is this AA

acidic

what classification is this AA

acidic

what classification is this AA

basic

what classification is this AA

basic

what classification is this AA

basic

what classification is this AA

sulfur

what classification is this AA

sulfur

what classification is this AA

sulfur

what classification is this AA

aromatic

what classification is this AA

aromatic

what classification is this AA

aromatic

what classification is this AA

1. enterkinase (endopeptidase) activates trypsinogen into trypsin. That active trypsin then activates chymotrypsinogen into chymotrypsin and procarboxypeptidase into carboxypeptidase

2. trypsin and chymotrypsin (endopeps) hydrolyze pep chains internally to create smaller chains. Then carboxypeptidase (exopep) breaks those into single AAs.

3. amino pep and dipep break off more singular AA for the other terminal end

describe the process of protein digestion in the smal intestine

direct absorption of di and tri peptides.

what is the “new method“ for amino acid absorption

dietary protein splits into 2 paths. one part becomes bypass protein that escapes the rumen and will later get digested/ used in the small intestine. the other becomes intake protein that gets fermented by mirobes. these proteins will be broken down into peptides, amino acids, ammonia

describe protein utilization in the rumen