Characterization of Glutamine Synthetase Isoforms from Chlorella
Ion-exchange chromatography of extracts derived from Chlorella sorokiniana mutant strain (oxygen resistant) yielded two separate activity peaks of glutamine synthetase (GS). $\text{GS}_{\text{I}}$ and $\text{GS}_{\text{II}}$ were purified 220- and 187-fold and have molecular weights of approximately...
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Veröffentlicht in: | Plant physiology (Bethesda) 1985-04, Vol.77 (4), p.791-794 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Ion-exchange chromatography of extracts derived from Chlorella sorokiniana mutant strain (oxygen resistant) yielded two separate activity peaks of glutamine synthetase (GS). $\text{GS}_{\text{I}}$ and $\text{GS}_{\text{II}}$ 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 $\text{GS}_{\text{I}}$ and 43,000 for $\text{GS}_{\text{II}}$. The amino acid composition, catalytic, and immunological properties for both enzymes are similar. |
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ISSN: | 0032-0889 1532-2548 |
DOI: | 10.1104/pp.77.4.791 |