Purification and characterization of calmodulin from sea urchin spermatozoa.
Calmodulin was purified to apparent homogeneity from sea urchin spermatozoa by heat-treatment at 85 degrees C, ammonium sulphate precipitation at pH 4.2, DEAE-Sephacel chromatography and gel filtration on Sephadex G-100. Approximately 8.3 micrograms calmodulin were recovered per 10(10) sperm cells. The sperm calmodulin had an apparent molecular weight of 17 800. The purified calmodulin activated calmodulin-deficient phosphodiesterase from pig coronary arteries, with half-maximal activation occurring at approximately 40 ng calmodulin/ml. Trifluoperazine also inhibited the sperm calmodulin activity. These results demonstrate that calmodulin is present in high amounts in sea urchin spermatozoa, and that it is essentially the same as the calmodulin isolated from various other tissues.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D002147:Calmodulin / Q000302:isolation & purification* / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D008297:Male; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D012617:Sea Urchins / Q000032:analysis*; D013094:Spermatozoa / Q000032:analysis*
D000596:Amino Acids; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D010727:Phosphoric Diester Hydrolases