Further studies on the quaternary structure of yeast casein kinase II. 1986

R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior

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.

UI MeSH Term Description Entries
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D012269 Ribosomal Proteins Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits. Proteins, Ribosomal,Ribosomal Protein,Protein, Ribosomal
D012270 Ribosomes Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION. Ribosome
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular
D047388 Casein Kinases A group of protein-serine-threonine kinases that was originally identified as being responsible for the PHOSPHORYLATION of CASEINS. They are ubiquitous enzymes that have a preference for acidic proteins. Casein kinases play a role in SIGNAL TRANSDUCTION by phosphorylating a variety of regulatory cytoplasmic and regulatory nuclear proteins. Casein Kinase,Kinase, Casein,Kinases, Casein

Related Publications

R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
January 1987, Biomedica biochimica acta,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
September 1995, Comptes rendus de l'Academie des sciences. Serie III, Sciences de la vie,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
January 1945, Zeitschrift fur Immunitatsforschung und experimentelle Therapie,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
May 1997, The Journal of biological chemistry,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
February 2006, The Journal of biological chemistry,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
January 1994, Cellular & molecular biology research,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
January 1983, Methods in enzymology,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
July 1991, The Journal of biological chemistry,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
February 1993, Journal of cell science,
R Szyszka, and W Lopaczyński, and W Gałasiński, and N Grankowski, and E Gasior
July 1959, Toxicology and applied pharmacology,
Copied contents to your clipboard!