Töpfer-Petersen E, Henschen A
Department of Dermatology, University of Munich, FRG.
FEBS Lett. 1987 Dec 21;226(1):38-42. doi: 10.1016/0014-5793(87)80546-x.
The major fucose-binding protein of 53 kDa from boar spermatozoa was isolated to apparent homogeneity using a two-step procedure including high-performance gel filtration and reversed-phase chromatography. The N-terminal sequence of the protein revealed that it is identical with the sperm proteinase acrosin. By means of a solid-phase zona-binding assay based on the avidin-biotin system it was demonstrated that acrosin also interacts strongly with porcine zona pellucida. Thus, the acrosin molecule combines specific proteolytic activity with zona- and carbohydrate-affinity properties, i.e. previously unrecognized properties of a serine proteinase. It seems likely that this special affinity of acrosin directs the proteolytic activity to its structural target in the vivo situation.
采用包括高效凝胶过滤和反相色谱在内的两步法，从公猪精子中分离出了表观均一的53 kDa主要岩藻糖结合蛋白。该蛋白的N端序列显示，它与精子蛋白酶顶体蛋白酶相同。通过基于抗生物素蛋白-生物素系统的固相透明带结合试验表明，顶体蛋白酶也与猪透明带强烈相互作用。因此，顶体蛋白酶分子将特定的蛋白水解活性与透明带和碳水化合物亲和特性结合在一起，即丝氨酸蛋白酶以前未被认识的特性。在体内情况下，顶体蛋白酶的这种特殊亲和力似乎将其蛋白水解活性导向其结构靶点。
