BIOL 4350 Lecture Notes - Lecture 7: Carbamoyl Phosphate, Ornithine, Mitochondrial Matrix

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6 Feb 2017

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FEBRUARY 1 PPT 4 (10-end) PPT 5 (1-7) LECTURE 7
-Give an amino acid and if you transaminated this amino acid and that amino acid to see what would
Glutamate Dehydrogenase
- Redox reaction for glutamate
- Oxidizes glutamate to create alpha-ketoglutarate
o Alpha ketoglutarate gets sent back to the urea cycle
o Get ammonia out of the reduction
Gets inserted in the mitochondrial matrix of a liver cell
- X dehdrogenase oidizes X
- Alanine and glutamine are 2 amino acids that act as amino-carriers to send excess amino acids to the
o Create ammonium off of the glutamate which eventually makes urea
- Carbamoyl phosphate
o Generated from ATP and bicarbonate and ammonia to form a carbamoyl phosphate
o Is a high energy molecule
o Enzyme that synthesizes is carbamoyl phosphate synthesase
o Incorporated into preexisting ornithine to create citrulline
Cleave off phosphate to join it with ornithine
Citrilline gets adenylated by adding 2 ATP to make high energy bond
The intermediate was formed by addition of another ATP
Aspartate was added and AMP was removed to for argninosuccinate
Fumarate gets removed and left with arginine
Hydrolyze arginine to form urea and ornithine which restarts the cycle
Takes place partially in the mitochondrial matrix and partially in the cytosol
2 ATP were used in total for the cycle
o What you need to know:
Shrink it down and put it on the card and understand the basic mechanism
- Glutamine and alanine carry ammonia from extrahepatic tissues to the liver
o Important blood carrier groups for nitrogen to the liver
o Pruate uilds up as ou’re orking
Carbon skeleton of alanine
o To use pyruvate, you need to do aerobic respiration
- Electrophoresismolecules are separated by their velocity in an electric field
SDSnegatively charged denaturing detergent
BMEbetamercaptoethanol breaks disulfide bonds
o Separation strictly by size
- Isoelectric focusing
o Create a gel with a pH gradient (from 3 to 9)
o Load protein sample at pH 9 and apply electric field
Start moving down the tube and there is a pH gradient
Proteins stay in the same area as their isoelectric point
o Around pH 9, it is underprotonated (-)
o Around pH 3, it is overprotonated (+)
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