Multiple forms of glutamine synthetase in Bacillus brevis AG 4.
Glutamine synthetase in Bacillus brevis AG 4, a Gram-positive spore forming bacteria, has been found to exist in multiple molecular forms. It was purified to electrophoretic homogeneity by single-step Blue Sepharose affinity chromatography. The native enzyme has a molecular weight of 600,000 with subunits of 50,000. The enzyme samples purified from different stages of growth differed in Mg2+ sensitivity and other kinetic properties. Four different enzyme samples selected on the basis of Mg2+ sensitivity showed distinct mobilities at pH 6.3 on PAGE using discontinuous buffer system. A correlation amongst Mg2+ sensitivity, electrophoretic mobility, and kinetic properties was highly suggestive of multiple forms of glutamine synthetase in Bacillus brevis arising due to modification.
Tiwari
R P
RP
Gaur
N K
NK
Garg
G K
GK
D001407:Bacillus / Q000201:enzymology* / Q000254:growth & development; D005974:Glutamate-Ammonia Ligase / Q000302:isolation & purification*; D007527:Isoenzymes / Q000302:isolation & purification; D007700:Kinetics
D007527:Isoenzymes; D005974:Glutamate-Ammonia Ligase