Jonáková V, Calvete J J, Mann K, Schäfer W, Schmid E R, Töpfer-Petersen E
Institute of Molecular Genetics, Czechoslovak Academy of Scïences, Praha.
FEBS Lett. 1992 Feb 3;297(1-2):147-50. doi: 10.1016/0014-5793(92)80347-j.
Acrosin inhibitors of seminal vesicle origin, after binding to their acceptor molecules on the anterior part of ejaculated sperm, are thought to be important capacitation factors, protecting zona binding sites during sperm uterine passage, and then dissociating to allow sperm binding to the zona pellucida of the oocyte. Each species so far tested possess an heterogeneous population of isoinhibitors which may display overlapping but not identical biological functions. Here we report the complete primary structure of three isoforms of a boar sperm-associated acrosin inhibitor, whose sequences are 90% identical to the seminal plasma counterpart. Despite this high analogy, the differences between the sperm-associated and the seminal plasma inhibitors may confer to them different physico-chemical properties which are postulated to be of functional importance.
精囊来源的顶体蛋白酶抑制剂，在与射出精子前部的受体分子结合后，被认为是重要的获能因子，在精子通过子宫时保护与透明带结合的位点，然后解离以允许精子与卵母细胞的透明带结合。到目前为止测试的每个物种都具有异质性的同工抑制剂群体，它们可能表现出重叠但不相同的生物学功能。在此，我们报道了一种公猪精子相关顶体蛋白酶抑制剂三种同工型的完整一级结构，其序列与精浆中的对应物有90%的同一性。尽管有这种高度相似性，但精子相关抑制剂和精浆抑制剂之间的差异可能赋予它们不同的物理化学性质，据推测这些性质具有功能重要性。
