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PMID: 2751663 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A nuclear casein type II kinase from maize endosperm phosphorylating HMG proteins.

Biochemical and biophysical research communications ·Vol. 162 ·No. 1 ·1989-07-14 ·Pages 456-63

Grasser KD, Maier UG, Feix G

Abstract

A casein kinase of the type II was isolated and enriched from nuclear lysates of maize endosperm tissue. The kinase activity requires 10 mM Mg2+ for maximal activity, can utilize either ATP or GTP as phosphate donors and is inhibited by polyamines, heparin and monovalent cations. A substrate specificity of the kinase activity towards specific nuclear proteins is indicated by its phosphorylation of high mobility group (HMG) proteins isolated from endosperm and its lack of accepting histones as protein substrates.

MeSH Terms
Animals Casein Kinases Cattle Chromatography, Agarose High Mobility Group Proteins/metabolism Kinetics Nuclear Proteins/metabolism,physiology Phosphorylation Plant Proteins/metabolism Protein Kinases/metabolism,physiology Sepharose/analogs & derivatives Substrate Specificity Zea mays/enzymology
Chemicals
High Mobility Group Proteins Nuclear Proteins Plant Proteins heparin-sepharose Sepharose Protein Kinases Casein Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Grasser K D
Institute for Biology III, Albert-Ludwigs-Universität, Freiburg, FRG.
Maier U G
Feix G
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1989-07-14
Pages
456-63
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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