PMID: 6161607Aug 1, 1980Paper

The binding of calmodulin to myelin basic protein and histone H2B

The Biochemical Journal
R J Grand, S V Perry

Abstract

1. A calmodulin-binding protein of apparent mol.wt. 19 000 has been purified from chicken gizzard. Similar proteins have been isolated from bovine uterus, rabbit skeletal muscle and rabbit liver. 2. These proteins migrated as an equimolar complex with bovine brain calmodulin on electroporesis on polyacrylamide gels in the presence of Ca2+ and 6M-urea. The complex was dissociated in the presence of EGTA. 2. The chicken gizzard calmodulin-binding protein has been shown to be identical with chicken erythrocyte histone H2B on the basis of partial amino acid sequence determination. 4. The calmodulin-binding proteins of apparent mol.wt. 22 000 isolated previously from bovine brain [Grand & Perry (1979) Biochem. J. 183, 285-295] has been shown, on the basis of partial amino-acid-sequence determination, to be identical with myelin basic protein. 5. The activation of bovine brain phosphodiesterase by calmodulin is inhibited by excess bovine uterus calmodulin-binding protein (histone H2B). 6. The phosphorylation of myelin basic protein by phosphorylase kinase is partially inhibited, whereas the phosphorylation of uterus calmodulin-binding protein (histone H2B) is unaffected by calmodulin or troponin C. 7. The subcellular distribution of ...Continue Reading

Citations

Dec 1, 2009·Journal of Thrombosis and Haemostasis : JTH·A A KondkarP F Bray
Feb 24, 1992·FEBS Letters·A de LilloJ F Fierro
Sep 14, 1981·FEBS Letters·K SobueS Kakiuchi
Sep 18, 2002·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·David S Libich, George Harauz
Apr 1, 1990·Journal of Muscle Research and Cell Motility·A Sobieszek
Apr 10, 1989·FEBS Letters·J F FierroC Hardisson
Oct 1, 1983·Biochemical Pharmacology·M S BarnetteB Weiss
Nov 22, 1983·Biochimica Et Biophysica Acta·G M PolyaV Micucci
Jan 1, 1988·Progress in Neurobiology·J B Ulmer
Jan 1, 1983·Neurochemistry International·S Kakiuchi
Jun 14, 1985·Biochemical and Biophysical Research Communications·J R McDonald, M P Walsh

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