ISSN 2415-1297 (Online)   ISSN 2415-1300 (Print)
 
             
 
Volume : 31 Issue : 1 Year : 2024
 
Ammonia Assimilation in Methanobacterium Formicium and Some Properties of Glutamine Synthetase [Med J Islamic World Acad Sci]
Med J Islamic World Acad Sci. 1993; 6(2): 118-120

Ammonia Assimilation in Methanobacterium Formicium and Some Properties of Glutamine Synthetase

Raquya Siddiqi, John P. Robinson
From Department of Microbiology, University of Karachi, Karachi- 75270, Pakistan.

Since Methanobacterium formicium grew in the presence of low ammonia concentration it was thought likely that GS/GOGAT system for ammonia assimilation would be present in cell extract of M. formicium. Cell free extracts of M. formicium were assayed by -glutamyl transferase method. The cell free extracts preparation showed significant glutamine synthetase activity. Optimum pH of glutamine synthetase was found to be 8.8. The enzyme was partially oxygen sensitive and temperature sensitive. Glutamate synthase (GOGAT) activity could not be detected in cell free extracts of M. formicium. Glutamate dehydrogenase activity was present in cells grown with high concentration (3.4 mM) of ammonia.

Keywords: Ammonia assimilation, glutamine synthetase, M. formicium.


Raquya Siddiqi, John P. Robinson. Ammonia Assimilation in Methanobacterium Formicium and Some Properties of Glutamine Synthetase. Med J Islamic World Acad Sci. 1993; 6(2): 118-120

Corresponding Author: Raquya Siddiqi, Pakistan


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