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.
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Authors | R J Wanders, J Ruiter, C W van Roermund, R B Schutgens, R Ofman, S Jurriaans, J M Tager |
Journal | Clinica 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 |
PMID | 2397596
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Glyoxylates
- Transaminases
- Alanine Transaminase
- Alanine-glyoxylate transaminase
- Alanine
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Topics |
- Alanine
(blood)
- Alanine Transaminase
(blood)
- Biopsy
- Glyoxylates
(blood)
- Humans
- Hydrogen-Ion Concentration
- Hyperoxaluria
(enzymology)
- Kinetics
- Liver
(enzymology)
- Spectrophotometry
- Transaminases
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