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Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method.

Abstract
We have studied the characteristics of human liver alanine-glyoxylate aminotransferase, which is deficient in hyperoxaluria type I, an inherited disorder of glyoxylate metabolism. The enzyme was optimally active at pH 8.0 showing apparent Km values for L-alanine and glyoxylate of 8.3 and 1.3 mmol/l, respectively. Activity was found to proceed linearly for up to 4 h. Measurements under these optimal conditions enabled the biochemical diagnosis of hyperoxaluria type I to be made via enzyme activity measurements in percutaneous needle biopsy specimens of liver tissue.
AuthorsR J Wanders, J Ruiter, C W van Roermund, R B Schutgens, R Ofman, S Jurriaans, J M Tager
JournalClinica chimica acta; international journal of clinical chemistry (Clin Chim Acta) Vol. 189 Issue 2 Pg. 139-44 (Aug 15 1990) ISSN: 0009-8981 [Print] Netherlands
PMID2397596 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Glyoxylates
  • Transaminases
  • Alanine Transaminase
  • Alanine-glyoxylate transaminase
  • Alanine
Topics
  • Alanine (blood)
  • Alanine Transaminase (blood)
  • Biopsy
  • Glyoxylates (blood)
  • Humans
  • Hydrogen-Ion Concentration
  • Hyperoxaluria (enzymology)
  • Kinetics
  • Liver (enzymology)
  • Spectrophotometry
  • Transaminases

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