Activities | Families | Sequences | Fold types | References | Help
B6db references: 91312840

type Journal Article
authors Mawal, M. R.; Deshmukh, D. R.
title Purification and properties of alpha-aminoadipate aminotransferase from rat kidney
journal Prep Biochem
ui 91312840
year (1991)
volume 21
number 1
pages 63-73
keywords Animal
abstract 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.
last changed 2002/11/12 16:17

B6db references