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B6db references: 82183052

type Journal Article
authors Okuno, E.; Minatogawa, Y.; Kido, R.
title Co-purification of alanine-glyoxylate aminotransferase with 2- aminobutyrate aminotransferase in rat kidney
journal Biochim Biophys Acta
Activity 2.6.1.44
Family 2.6.1.44.a
sel selected
ui 82183052
year (1982)
volume 715
number 1
pages 97-104.
 
keywords 4-Aminobutyrate Transaminase/*isolation & purification/metabolism
abstract Alanine-glyoxylate aminotransferase and 2-aminobutyrate aminotransferase were co-purified from rat kidney to a single protein (about 500-fold purified from the homogenate). The activity ratios of alanine-glyoxylate aminotransferase to 2-aminobutyrate aminotransferase were constant during co-purification steps suggesting the 2- aminobutyrate aminotransferase activity was catalysed by only alanine- glyoxylate aminotransferase. The molecular weight of the enzyme was estimated to be approx. 213 000, 220 000 and 236 000 by analytical ultracentrifugation, Sephadex G-150 gel filtration and sucrose density gradient centrifugation, respectively. From the polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate, the enzyme consisted of four apparently similar subunits having a molecular weight of approx. 56 000. The enzyme was almost specific to L-alanine and L-2- aminobutyrate as amino donor and to glyoxylate, pyruvate and 2- oxobutyrate as amino acceptor. The enzyme was identified with rat liver alanine-glyoxylate aminotransferase isoenzyme 2 but not with rat liver alanine-glyoxylate aminotransferase isoenzyme 1 from Ouchterlony double diffusion analysis. Absorption spectra and some kinetic properties of the enzyme were clarified.
last changed 2010/09/02 13:02

B6db references