Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and Synechococcus
- 1 March 1989
- journal article
- research article
- Published by Springer Nature in Carlsberg Research Communications
- Vol. 54 (2), 67-79
- https://doi.org/10.1007/bf02907586
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.Keywords
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