Isolation and partial characterization of a protein kinase NII from wheat germ chromatin |
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Authors: | Antonella Angiolillo Fausto Panara Gina Piccinini Gian Luigi Gianfranceschi |
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Affiliation: | (1) Istituto di Biologia Cellulare, Universita' di Perugia, via Elce di sotto, I-06100 Perugia, Italia |
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Abstract: | 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 of histone proteins. Polypeptide bands at 46 kDa, 37 kDa and 25 kDa were estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Autophosphorylation of the 25 kDa subunit was observed following incubation of the purified kinase with ( -32P)ATP and ( -32P)GTP. |
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Keywords: | phosphorylation protein kinase NII wheat germ chromatin |
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