Multiple forms of glutamine synthetase in Bacillus brevis AG 4.
Indian J Biochem Biophys
;
1989 Feb; 26(1): 43-7
Article
in English
| IMSEAR
| ID: sea-26299
ABSTRACT
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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Bacillus
/
Kinetics
/
Glutamate-Ammonia Ligase
/
Isoenzymes
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1989
Type:
Article
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