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Isolation and purification of a new 105 kDa protein kinase from rat liver nuclei.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 1982 May 03; Vol. 703 (2), pp. 171-9. - Publication Year :
- 1982
-
Abstract
- A protein kinase was purified from rat liver nuclei by affinity chromatography on poly(L-lysine)-agarose and protein kinase inhibitor-Sepharose 4B columns. The relative molecular weight of this protein kinase is 105000 (determined by 10% SDS-polyacrylamide slab gel electrophoresis, gel filtration on Sephadex G-200 and sedimentation velocity ultracentrifugation). Its pH optimum is between 8.0 and 9.0. It is active over a wide range of mg2+ concentrations, and its activity is stimulated by several small acidic proteins (calmodulin, lactalbumin, parvalbumin, protein kinase inhibitor and troponin C). The enzyme phosphorylates a variety of substrates including casein, histones, protamine and the synthetic basic polypeptides, poly(L-arginine) and poly(L-lysine).
- Subjects :
- Adenosine Triphosphate metabolism
Animals
Cations, Divalent pharmacology
Cell Nucleus enzymology
Chromatography, Affinity methods
Chromatography, Gel
Chromatography, Ion Exchange
Male
Molecular Weight
Polylysine
Rats
Rats, Inbred Strains
Liver enzymology
Protein Kinases isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 703
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 7082680
- Full Text :
- https://doi.org/10.1016/0167-4838(82)90045-0