Purification and properties of alpha-aminoadipate aminotransferase from rat kidney.
Previous studies with rat kidney preparations indicated that alpha-aminoadipate aminotransferase (AadAT) and kynurenine aminotransferase (KAT) activities are associated with a single protein. However, recent studies from our laboratory demonstrated that AadAT and KAT activities belong to two different proteins. AadAT from rat kidney supernatant fraction was purified by affinity chromatography to electrophoretic homogeneity. This rapid and efficient procedure improved the yield and the degree of purification over previously published methods and separated AadAT from KAT. The molecular weight of the enzyme was estimated to be 89,000 by Sephadex G-200 gel filtration chromatography. SDS-PAGE indicated that the enzyme is composed of two apparently identical subunits. Absorption spectra and the kinetic properties of AadAT are reported.
Mawal
M R
MR
Department of Pediatrics, Children's Hospital of Michigan, Wayne State University, Detroit 48201.
Deshmukh
D R
DR
D051307:2-Aminoadipate Transaminase; D000818:Animals; D003998:Dicarboxylic Acids / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D000637:Transaminases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*
D003998:Dicarboxylic Acids; D000637:Transaminases; D051307:2-Aminoadipate Transaminase