Modification of glutamine synthetase in Bacillus brevis AG 4.
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.
Tiwari
R P
RP
Rathore
V S
VS
Garg
G K
GK
D000469:Alkaline Phosphatase; D001345:Autoradiography; D001407:Bacillus / Q000201:enzymology*; D005974:Glutamate-Ammonia Ligase / Q000032:analysis*; D007120:Immunochemistry; D010727:Phosphoric Diester Hydrolases
D000469:Alkaline Phosphatase; D010727:Phosphoric Diester Hydrolases; D005974:Glutamate-Ammonia Ligase