Garbers D L, Hansbrough J R, Radany E W, Hyne R V, Kopf G S
J Reprod Fertil. 1980 Jul;59(2):377-81. doi: 10.1530/jrf.0.0590377.
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.
通过85℃热处理、pH 4.2硫酸铵沉淀、DEAE-葡聚糖凝胶柱层析以及Sephadex G-100凝胶过滤，从海胆精子中纯化出了纯度看似很高的钙调蛋白。每10¹⁰个精子细胞中大约可回收8.3微克钙调蛋白。精子钙调蛋白的表观分子量为17800。纯化后的钙调蛋白激活了来自猪冠状动脉的钙调蛋白缺陷型磷酸二酯酶，约40纳克钙调蛋白/毫升时出现半数最大激活。三氟拉嗪也抑制精子钙调蛋白的活性。这些结果表明，钙调蛋白在海胆精子中大量存在，并且它与从其他各种组织中分离出的钙调蛋白基本相同。
