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B6db references: diqcgsa

type Journal Article
authors Nair, S. P.; Harwood, J. L.; John, R. A.
title Direct identification and quantification of the cofactor in glutamate semialdehyde aminotransferase from pea leaves
journal FEBS Lett
ui Diqcgsa
year (1991)
volume 283
number 1
pages 4-6
keywords Chromatography, Gel
abstract Glutamate semialdehyde aminotransferase, a key enzyme in the synthetic pathway leading to chlorophyll was purified from pea (Pisum sativum) leaves. Although the preparation contained a single contaminant the enzyme could be unambiguously identified as a dimer of subunit molar mass 45 kDa having an absorption spectrum consistent with the presence of pyridoxamine phosphate as cofactor. The cofactor was released by treatment with strong phosphate at low pH and was identified and quantified fluorimetrically. The specific activity of the enzyme (1.4; 23 is very much higher than previously reported.
last changed 2008/05/21 16:26

B6db references