Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus.
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Grimm B, Bull A, Welinder KG, Gough SP, Kannangara CG
Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus.
Carlsberg Res Commun. 1989;54(2):67-79.
- PubMed ID
- 2505791 [ View in PubMed]
- 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.