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. 1985 Apr;77(4):791-4.
doi: 10.1104/pp.77.4.791.

Characterization of glutamine synthetase isoforms from chlorella

R F Beudeker  1 , F R Tabita
Affiliations

Characterization of glutamine synthetase isoforms from chlorella

R F Beudeker et al. Plant Physiol. 1985 Apr.

Abstract

Ion-exchange chromatography of extracts derived from Chlorella sorokiniana mutant strain (oxygen resistant) yielded two separate activity peaks of glutamine synthetase (GS). GS(I) and GS(II) were purified 220- and 187-fold and have molecular weights of approximately 398,000 and 360,000, respectively. Both enzymes are composed of eight identical subunits with a subunit molecular weight of 47,000 for GS(I) and 43,000 for GS(II). The amino acid composition, catalytic, and immunological properties for both enzymes are similar.

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