Expression of three plant glutamine synthetase cDNA in Escherichia coli. Formation of catalytically active isoenzymes, and complementation of a glnA mutant.

doi:10.1111/j.1432-1033.1990.tb19340.x

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Article

Expression of three plant glutamine synthetase cDNA in Escherichia coli. Formation of catalytically active isoenzymes, and complementation of a glnA mutant.

European journal of biochemistry - 24 Oct 1990

Bennett M, Cullimore J

Abstract excerpt

Three cDNA clones encoding the closely related glutamine synthetase (GS) alpha, beta and gamma polypeptides of Phaseolus vulgaris (French bean) were recombinantly expressed in Escherichia coli. The GS expression plasmids correctly synthesised the recombinant alpha, beta and gamma polypeptides which then assembled into catalytically active homo-octameric isoenzymes. These isoenzymes behaved similarly to their...

Topics

Base Sequence
Chromatography, Gel
Chromatography, Ion Exchange
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Enzyme Stability
Escherichia coli
Fabaceae
Genetic Complementation Test
Glutamate-Ammonia Ligase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Isoenzymes

Molecular Sequence Data

Mutation

Plants, Medicinal

Plasmids

Recombinant Proteins

Solubility

Source

Open in PubMed

Identifiers

PMID: 1977583
DOI: 10.1111/j.1432-1033.1990.tb19340.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1977583-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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