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• W1982129358 abstract "Boar and stallion seminal plasmas were fractionated using affinity chromatography on heparin-Sepharose. In both species, among other proteins, the heparin-binding (H+) and non-heparin-binding (H−) fractions each contained glycoforms of either porcine PSP-I or equine HSP-I and HSP-2. However, porcine H+/PSP-I eluted as a monomeric protein, whereas H−/PSP-I formed a heterodimer with PSP-II, another major seminal plasma protein. On the other hand, the stallion proteins H+/HSP-1 and H+/HSP-2 eluted together as an aggregate of relative molecular mass (Mr) 90 000, whereas H−/HSP-1 and H−/HSP-2 eluted as monomers (15 000). Remarkably, when PSP-I and PSP-II from the H− fraction were separated, both proteins bound to heparin. Altogether these data show that glycosylation has an indirect effect on the heparin-binding ability of PSP-I, HSP-1 and HSP-2 through modulation of their aggregation state." @default.
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• W1982129358 date "1995-09-01" @default.
• W1982129358 modified "2023-10-14" @default.
• W1982129358 title "Effect of glycosylation on the heparin-binding capability of boar and stallion seminal plasma proteins" @default.
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• W1982129358 doi "https://doi.org/10.1016/0021-9673(95)00011-b" @default.
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