Reference "Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus"

Reference ID

8645

Title

Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus

Source

Carlsberg Res Commun, 1989, vol. 54, pp. 67-79

Authors (5)

Grimm-B	Bull-A
Welinder-K-G	Gough-S-P
Kannangara-C-G

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.