PMID: 6163425Sep 1, 1980Paper

Interactions of basic polypeptides and proteins with calmodulin

The Biochemical Journal
T ItanoJ T Penniston

Abstract

Low concentrations (less than 10 microgram/ml) of a number of highly basic polypeptides inhibit the calmodulin-stimulated cyclic nucleotide phosphodiesterase. Inhibitory compounds include synthetic polypeptides [polylysine (D and L) and polyarginine] and basic proteins (protamine, histones H1, H2A, H2B, H3 and H4 and myelin basic protein). Polylysine of mol.wt. about 2000 or higher was inhibitory, but pentalysine did not inhibit. Other basic proteins and compounds did not inhibit, including bradykinin, spermine and putrescine. In mixtures of calmodulin and basic protein, complexes were formed whether Ca2+ was present or not. This was true for polylysine, myelin basic protein and histone H2B. These interactions suggest that the inhibition of the phosphodiesterase is due to interaction of these basic proteins with calmodulin. The wide variety of basic polypeptides and proteins that affect the calmodulin stimulation of phosphodiesterase indicates that these interactions are not specific.

Citations

Nov 28, 2006·International Journal of Food Sciences and Nutrition·Huan Li, Rotimi E Aluko
Jan 21, 2012·Journal of Food Science·Chibuike C Udenigwe, Rotimi E Aluko
Aug 1, 1981·Cell Calcium·F F Vincenzi
Oct 1, 1996·Journal of Dairy Science·K KizawaU Murakami
Jan 1, 1986·The Journal of Membrane Biology·J H Crabb, R C Jackson
Jan 1, 1980·Annals of the New York Academy of Sciences·J T PennistonT Itano
Sep 18, 2002·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·David S Libich, George Harauz
Jan 17, 1983·European Journal of Biochemistry·B M AmiranoffG E Rosselin
Jul 14, 2005·Molecular and Cellular Biochemistry·G Vani, C S Shyamala Devi
Apr 1, 1984·The Journal of Dermatology·Y KusakabeT Yamauchi
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