Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method.
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.
Department of Pediatrics, University Hospital Amsterdam, The Netherlands.
R J
RJ
Wanders
J
J
Ruiter
C W
CW
van Roermund
R B
RB
Schutgens
R
R
Ofman
S
S
Jurriaans
J M
JM
Tager
D000409:Alanine / Q000097:blood; D000410:Alanine Transaminase / Q000097:blood*; D001706:Biopsy; D006038:Glyoxylates / Q000097:blood; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006959:Hyperoxaluria / Q000201:enzymology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D013053:Spectrophotometry; D000637:Transaminases
D006038:Glyoxylates; D000637:Transaminases; D000410:Alanine Transaminase; C019635:Alanine-glyoxylate transaminase; D000409:Alanine