Modification of glutamine synthetase in Bacillus brevis AG 4.
Indian J Biochem Biophys
;
1989 Feb; 26(1): 48-51
Article
in English
| IMSEAR
| ID: sea-29048
ABSTRACT
The various forms of glutamine synthetase obtained from Bacillus brevis have been found to be antigenically identical. Alkaline phosphatase treatment of the fast moving form (GS4) reduced the electrophoretic mobility of the enzyme. Radiolabelling and autoradiographic studies have also indicated that 32P-incorporation is high in the form depicting high Rm value. Thus, it appears that these forms arise due to covalent modification of the enzyme involving a phosphate group.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Autoradiography
/
Bacillus
/
Immunochemistry
/
Phosphoric Diester Hydrolases
/
Alkaline Phosphatase
/
Glutamate-Ammonia Ligase
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1989
Type:
Article
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