Casein kinase II of yeast contains two distinct alpha polypeptides and an unusually large beta subunit
Casein kinase II of yeast has been purified to near homogeneity by a procedure which includes affinity chromatography on heparin-agarose. The purified enzyme consists of four polypeptides with molecular weights of 42,000, 41,000, 35,000, and 32,000. The 42,000- and 35,000-Da polypeptides are immunol...
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Veröffentlicht in: | The Journal of biological chemistry 1987-02, Vol.262 (4), p.1829-1835 |
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Format: | Artikel |
Sprache: | eng |
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