Characterization of Glutamine Synthetase Isoforms from Chlorella | Zendy

R. F. Beudeker | Zendy; F. Robert Tabita | Zendy

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Characterization of Glutamine Synthetase Isoforms from Chlorella

Author(s) -

R. F. Beudeker,

F. Robert Tabita

Publication year - 1985

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.77.4.791

Subject(s) - glutamine synthetase , glutamine , biochemistry , biology , enzyme , protein subunit , chlorella , chlorella sorokiniana , mutant , amino acid , molecular mass , strain (injury) , gene , botany , algae , anatomy

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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