Bonnet F, Perin J P, Maillet P, Jolles P, Alliel P M
Laboratoire des Protéines, URA C.N.R.S. No. 1188, Université de Paris V, France.
Biochem J. 1992 Dec 1;288 ( Pt 2)(Pt 2):565-9. doi: 10.1042/bj2880565.
A glycosaminoglycan-bearing polypeptide (S.GP), present in human seminal plasma, was purified to homogeneity by a combination of CsCl density-gradient centrifugation, f.p.l.c. ion-exchange chromatography on a Mono Q HR column and Superose 6 gel filtration. The observed polydispersity of S.GP was attributed to the heterogeneity of its glycosaminoglycan content. Enzymic deglycosylation experiments and N-terminal amino-acid sequence determination indicate that it consists of a polypeptide (apparent molecular mass approx. 18 kDa) bearing both chondroitin and heparan sulphate chains. Evidence is given that S.GP contains a glycosaminoglycan-linkage domain of a so far uncharacterized gene product, proteolytically processed in the genital tract.
通过氯化铯密度梯度离心、在Mono Q HR柱上进行快速蛋白质液相色谱离子交换色谱以及Superose 6凝胶过滤相结合的方法，对存在于人类精浆中的一种携带糖胺聚糖的多肽（S.GP）进行了纯化，直至达到均一性。观察到的S.GP的多分散性归因于其糖胺聚糖含量的异质性。酶促去糖基化实验和N端氨基酸序列测定表明，它由一个携带软骨素和硫酸乙酰肝素链的多肽（表观分子量约为18 kDa）组成。有证据表明，S.GP包含一种迄今未鉴定的基因产物的糖胺聚糖连接结构域，该结构域在生殖道中进行蛋白水解加工。
