TY  - CHAP
M1  - Book, Section
TI  - Catabolism of Proteins & of Amino Acid Nitrogen
A1  - Rodwell, Victor W.
A2  - Rodwell, Victor W.
A2  - Bender, David A.
A2  - Botham, Kathleen M.
A2  - Kennelly, Peter J.
A2  - Weil, P. Anthony
PY  - 2018
T2  - Harper's Illustrated Biochemistry, 31e
AB  - OBJECTIVESAfter  studying  this  chapter,  you  should  be  able  to:Describe  protein  turnover,  indicate  the  mean  rate  of  protein  turnover  in  healthy  individuals,  and  provide  examples  of  human  proteins  that  are  degraded  at  rates  greater  than  the  mean  rate.Outline  the  events  in  protein  turnover  by  both  ATP-dependent  and  ATP-independent  pathways,  and  indicate  the  roles  in  protein  degradation  played  by  the  proteasome,  ubiquitin,  cell  surface  receptors,  circulating  asialoglycoproteins,  and  lysosomes.Indicate  how  the  ultimate  end  products  of  nitrogen  catabolism  in  mammals  differ  from  those  in  birds  and  fish.Illustrate  the  central  roles  of  transaminases  (aminotransferases),  of  glutamate  dehydrogenase,  and  of  glutaminase  in  human  nitrogen  metabolism.Use  structural  formulas  to  represent  the  reactions  that  convert  NH3,  CO2,  and  the  amide  nitrogen  of  aspartate  into  urea,  and  identify  the  subcellular  locations  of  the  enzymes  that  catalyze  urea  biosynthesis.Indicate  the  roles  of  allosteric  regulation  and  of  acetylglutamate  in  the  regulation  of  the  earliest  steps  in  urea  biosynthesis.Explain  why  metabolic  defects  in  different  enzymes  of  urea  biosynthesis,  although  distinct  at  the  molecular  level,  present  similar  clinical  signs  and  symptoms.Describe  both  the  classical  approaches  and  the  role  of  tandem  mass  spectrometry  in  screening  neonates  for  inherited  metabolic  diseases.  
SN  - 
PB  - McGraw-Hill Education
CY  - New York, NY
Y2  - 2024/04/18
UR  - accesspharmacy.mhmedical.com/content.aspx?aid=1160190122
ER  -