Gietzen K, Galla H J
Biochem J. 1985 Aug 15;230(1):277-80. doi: 10.1042/bj2300277.
Seminalplasmin, a strongly basic protein isolated from bull semen, was found to antagonize with high potency and extraordinary specificity the function of calmodulin. Calmodulin antagonism is the result of an interaction between the two proteins, which is mainly determined by electrostatic forces. The stimulation of Ca2+-transporting ATPase and phosphodiesterase by calmodulin was half-maximally inhibited at approx. 0.1 microM-seminalplasmin. However, the basal activity of calmodulin-dependent enzymes was not significantly altered by seminalplasmin over the concentration range investigated.
精液纤溶酶是一种从公牛精液中分离出的强碱性蛋白质,它被发现能高效且特异拮抗钙调蛋白的功能。钙调蛋白拮抗作用是这两种蛋白质相互作用的结果,这种相互作用主要由静电力决定。在约0.1微摩尔精液纤溶酶存在时,钙调蛋白对钙离子转运ATP酶和磷酸二酯酶的刺激作用受到半数最大抑制。然而,在所研究的浓度范围内,精液纤溶酶并未显著改变钙调蛋白依赖性酶的基础活性。