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Partial purification and characterization of a second Calmodulin-activated Ca2+-dependent protein kinase from wheat germ

✍ Scribed by Gideon M. Polya; Vito Micucci

Book ID
113264691
Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
510 KB
Volume
785
Category
Article
ISSN
0167-4838

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A protein kinase, type NII, has been purified from wheat germ chromatin. The enzyme, which uses both ATP and GTP as phosphoryl donors, catalyzes the phosphorylation of casein, phosvitin and E. coli RNA polymerase, but not ofhistone proteins. Polypeptide bands at 46 kDa, 37 kDa and 25 kDa were estima