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Journal of Reproduction and Fertility (1980) 59 377-381
DOI: 10.1530/jrf.0.0590377
Copyright © 1980 Society for Reproduction and Fertility
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Purification and characterization of calmodulin from sea urchin spermatozoa

D. L. Garbers, J. R. Hansbrough, E. W. Radany, R. V. Hyne and G. S. Kopf

Summary. Calmodulin was purified to apparent homogeneity from sea urchin spermatozoa by heat-treatment at 85°C, ammonium sulphate precipitation at pH 4·2, DEAE-Sephacel chromatography and gel filtration on Sephadex G-100. Approximately 8·3 µg calmodulin were recovered per 1010 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.







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Copyright © 1980 by the Society for Reproduction and Fertility.