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Inactivation of glutamine synthetase by adenylylation in intact cells of E. coli.
Arch. Microbiol. 73, 97-103 (1970)
The adenine pool of a purineless mutant of E. coli was radioactively labelled by short incubation with 14C-adenine. The glutamine synthetase was inactivated in vivo by incubation of the cell suspension with 2x10-3 M NH4 + for 2 min. The inactivated glutamine synthetase was extracted from the cells and purified 20-fold. Incubation of the purified glutamine synthetase with phosphodiesterase regenerated the biosynthetic activity of the enzyme paralleled by the liberation of 14C-adenine and 14C-adenosine. 14C-adenine and 14C-adenosine were also obtained when inactivated glutamine synthetase, prepared in vitro by use of 14C-ATP and purified adenylylating enzyme, was incubated with phosphodiesterase under the same conditions. The similar liberation of adenine derivatives by phosphodiesterase from glutamine synthetase inactivated in a cell-free system as well as in intact cells, demonstrates that in both cases the inactivation consists in an adenylylation of the enzyme.
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Publication type
Article: Journal article
Document type
Scientific Article
ISSN (print) / ISBN
0003-9276
e-ISSN
1432-072X
Journal
Archives of Microbiology
Quellenangaben
Volume: 73,
Issue: 2,
Pages: 97-103
Publisher
Springer
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institut für Biochemie