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The intracellular localization of glutamine synthetase in Escherichia coli
Author(s) -
Sallal A.K.,
Abuharfeil N.M.,
Salim M.
Publication year - 2000
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/(sici)1521-4028(200005)40:2<127::aid-jobm127>3.0.co;2-k
Subject(s) - glutamine synthetase , differential centrifugation , biochemistry , glutamine , enzyme , cytoplasm , pronase , membrane , centrifugation , biology , intracellular , homogenization (climate) , microbiology and biotechnology , amino acid , trypsin , biodiversity , ecology
The major route of ammonia assimilation is the reaction which is catalysed by glutamine synthetase to give glutamine. Regulation and characterization of the enzyme in E. coli were done but not the localization. Cell‐free extracts and purified cytoplasmic membranes using differential centrifugation and density gradient techniques, were assayed for the percentage activity of the enzyme. Glutamine synthetase was detected in all cell‐free extracts of E. coli . 83% of the enzyme activity was found associated with the cytoplasmic membranes. Using monospecific glutamine synthetase antiserum and pronase, the major part of the enzyme was localized to the inside of the membranes and about 20% of the enzyme was found exposed to the outer surface.