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B6db references: 5059882

type Journal Article
authors Cooper, J. L.; Meister, A.
title Isolation and properties of highly purified glutamine transaminase
journal Biochemistry
sel selected
ui 5059882
year (1972)
volume 11
number 5
pages 661-71
keywords Amino Acids
abstract Glutamine transaminase has been obtained in highly purified form from rat liver. The isolated enzyme, which is apparently homogeneous by the criteria of ultracentrifugation S20,w= 6.25 S) and polyacrylamide gel electrophoresis, has a molecular weight of about 110,000. The enzyme exhibits absorbance maxima at 278 and 415 nm and the data indicate that the enzyme contains two subunits (mol wt -54,000). The enzyme is stabilized by a-keto acids and by 2-mercaptoethanol. Studies with 27 alpha-keto acids and 40 amino acids indicate that a-ketoglutaramate, a-keto-y-methiolbutyrate, P-mercaptopyruvate, glyoxylate, pyruvate, and Phydroxypyruvate are among the most active a-keto acid substrates, and that glutamine, glutamic acid gamma-ethyl ester, gamma-glutamylmethylamide, methionine, and ethionine are among the most active amino donors. The K, values for a number of the a-keto acids and amino acids, and the equilibrium constants for the glutamine-pyruvate, -glyoxylate, -alpha-keto-gamma-methiolbutyrate reactions were determined.
last changed 2009/04/28 09:53

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