Study your flashcards anywhere!

Download the official Cram app for free >

  • Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

How to study your flashcards.

Right/Left arrow keys: Navigate between flashcards.right arrow keyleft arrow key

Up/Down arrow keys: Flip the card between the front and back.down keyup key

H key: Show hint (3rd side).h key

A key: Read text to speech.a key

image

Play button

image

Play button

image

Progress

1/37

Click to flip

37 Cards in this Set

  • Front
  • Back
positive nitrogen balance
insulin world - anabolism
negative nitrogen balance
glucagon world - catabolism
Enzyme that breaks up protein in stomach
pepsin
Protein digestion in upper intestines
bicarb + proteases break peptides into AA or di & tripeptides (anything larger would produce Ab response in blood)
Proteases are _________
zyminogens
zyminogen
proteases are activated by cleavage
Cascade of protyolitic activation
Pepsinogen activated by high pH of stomach.
Trypsinogen activated by enteropeptidase (master key) into trypsin. Now tripsin (2nd key) activates all other enzymes (chymotrypsinogen, proelastase, procarboxypeptidase)
Where is enteropeptidase located?
wall of small intestine (damage can result in problems w/ protease activation)
why do we have so many enzymes in gut
each have particular specificity
Where do transporter proteins for amino acids exist?
intestinal luman and kidney
transporter proteins often work on specific amino acids T/F?
T
Nitrogen metabolism exists mostly in ______ world.
glucagon world
Where do 2 N in urea come from?
One as free N in form of ammonium
Other as N from aspartate
transamination
transfer of nitrogen. take an amino acid and turn it into alpha keto acid
cofactor used in transamination
PLP (vB6)
pyradoxal phosphate (B6)
enzyme that catalyzes transaminatin by accepting ammonium ion
glutamate-oxaloacetate transaminase/aspartate amino transferase (SGOT/AST)
transamination rxn
marker for liver damage
4C-5C
uses glutamate as N carrier
glutamate pyruvate transaminase/alanine aminotransferase (SGPT/ALT)
transamination rxn
enzyme is marker for liver damage
3C-5C
uses glutamate as N carrier
extracellular carrier of N
alanine
intracellular carrier of N
glutamate
What are sources of NH4+ (for urea) in liver :
1 free NH4+ & 1 from aspartate
Glutamate dehydrogenase
Takes N off glutamate (oxidative deamination) generating ammonium ion, NADPH, and a - ketoglutarate
hyperammonemia I
1) enzymes involved
2) clinical signs & syptoms
3) differential
ornathine transcarbamolase
ammonia levels will rise, BUN is going to go down as , glutamine is going to go up)***increase in uracil or orotic acid***
hyperammonemia II
1) enzymes involved
2) clinical signs & syptoms
3) differential
carbamoyl phosphate synthetase-
ammonia levels will rise, BUN is going to go down as , glutamine is going to go up***NO increase in uracil or orotic acid)***
urea precursors
amino acids
glutamate
aspartate
NH4+
N- acetyl glutamic acid
+ affector of urea cycle
Breakdown of AA takes place in peroxisome because
products are a-keto acid, H2O2 (toxic), and amonium ion
glutamine
can carry 2 N instead of just 1
Ammonia Toxicity
Ammonia level greater than 10 mgms/L is toxic to the cells
Ammonium Ion Blood level
0.5 mg/L
Ammonium Ion Blood level
0.5 mg/L
glutamine intracellular or extracellular
can be intracellular or extracellular carrier
intestinal cells have high concentrations of _______
glutamine (cuz rapidly dividing)
why do kidneys have high concentrations of glutamine
detoxification
carbamyl phosphyl sythetase 1 (CPSI)
found in mitochondria - ratel limiting step in protein digestion
N- acetyl glutamic acid
+ affector of urea cycle
stimulates CPS I enzyme
importance of ornithine & citruline
can cross mitochondrial membrane