Further studies on the quaternary structure of yeast casein kinase II.

Abstract

Casein kinase type II were isolated by the same procedure, from rat liver, human placenta, Querin carcinoma and yeast, and characterized. The mammalian enzymes were composed of three subunits alpha, alpha' and beta, whereas yeast kinase was composed of two subunits alpha and alpha'. It was shown that the catalytic activity, substrate and phosphate donor specificity, sensitivity to heparin and spermine were the same for all the kinases tested. The results give additional support to the suggestion [1] that the beta subunit is not required for optimal activity and specificity of yeast casein kinase II. The quaternary structure of the yeast enzyme of a molecular weight of approximately 150 000 is proposed as alpha2 alpha'2.

• Authors: R Szyszka, W Lopaczyński, W Gałasiński, N Grankowski, E Gasior
• Journal: Acta biochimica Polonica (Acta Biochim Pol) Vol. 33 Issue 1 Pg. 39-46 ( 1986) ISSN: 0001-527X [Print] Poland
• PMID: 3521166 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Macromolecular Substances
• Ribosomal Proteins
• Protein Kinases
• Casein Kinases

Topics

• Casein Kinases
• Electrophoresis, Polyacrylamide Gel
• Macromolecular Substances
• Protein Conformation
• Protein Kinases (isolation & purification)
• Ribosomal Proteins (isolation & purification)
• Ribosomes (ultrastructure)
• Saccharomyces cerevisiae (genetics)