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Isolation and partial characterization of a protein kinase NII from wheat germ chromatin

✍ Scribed by Antonella Angiolillo; Fausto Panara; Gina Piccinini; Gian Luigi Gianfranceschi

Publisher
Springer
Year
1991
Tongue
English
Weight
299 KB
Volume
15
Category
Article
ISSN
0301-4851

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✦ Synopsis

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 estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Autophosphorylation of the 25 kDa subunit was observed following incubation of the purified kinase with (7-32p)ATP and (7-32p)GTP.

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