Multiple forms of glutamine synthetase in Bacillus brevis AG 4.

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1989-02-01
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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.
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Tiwari RP, Gaur NK, Garg GK. Multiple forms of glutamine synthetase in Bacillus brevis AG 4. Indian Journal of Biochemistry & Biophysics. 1989 Feb; 26(1): 43-7
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https://imsear.searo.who.int/handle/123456789/26299
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Indian Journal of Biochemistry & Biophysics