Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C
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چکیده
منابع مشابه
Purification and characterization of echinoderm casein kinase II
Casein kinase II (CKII) is one of several protein kinases that become activated before germinal-vesicle breakdown in maturing sea-star oocytes. Echinoderm CKII was purified over 11000-fold with a recovery of -10% by sequential fractionation of the oocyte cytosol on tyrosine-agarose, heparin-agarose, casein-agarose and MonoQ. The purified enzyme contained 45, 38 and 28 kDa polypeptides, which co...
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Casein kinase I from broccoli was purified approximately 65,000-fold by chromatography on phosphocellulose, phenyl-Sepharose, CM-Sephacel, and affinity chromatography on N-(2-aminoethyl)-5-chloroisoquinolone-8-sulphonamide (CKI-7)-Sepharose. The catalytic subunit of casein kinase I was identified as a 36-38 kDa polypeptide doublet by using the technique of activity gel assay after SDS/PAGE with...
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Of the recently described members of the protein kinase C (PKC) family (-6, -6, -c), no detailed properties of the purified enzymes have been presented. Here we describe the expression of PKC-c in insect cells using a baculovirus vector. The recombinant enzyme has been purified to homogeneity by sequential chromatography on DEAE-cellulose, serine-Sepharose, Mono Q, and Superose 12; the protein ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1992
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2830829