type	Journal Article
authors	Grimm, B.; Bull, A.; Welinder, K. G.; Gough, S. P.; Kannangara, C. G.
title	Purification and partial amino acid sequence of the glutamate 1- semialdehyde aminotransferase of barley and synechococcus
journal	Carlsberg Res Commun
Activity	5.4.3.8
Family	5.4.3.8
ui	89374545
year	(1989)
volume	54
number	2
pages	67-79
keywords	Amino Acid Sequence
abstract	Glutamate-1-semialdehyde aminotransferase (E.C. 5.4.3.8) was purified from barley and the cyanobacteria Synechococcus PCC 6301. The purification procedure involved serial affinity chromatography and preparative polyacrylamide gel electrophoresis under non-denaturing conditions. The aminotransferase of these two organisms showed different mobilities in non-denaturing gels. In SDS-PAGE the enzyme from both organisms migrated as a single protein with an apparent molecular weight of 46.000 Da. An antibody against the barley enzyme cross-reacted with the cyanobacterial aminotransferase. This antibody also recognized a 17 kDa peptide cleaved from the barley protein with cyanogen bromide. Amino acid sequences of the NH2-termini revealed significant homology between the eucaryotic and cyanobacterial enzyme.
last changed	2008/05/21 16:26