Effect of glycosylation on the heparin-binding capability of boar and stallion seminal plasma proteins.

@article{Calvete1995EffectOG,
  title={Effect of glycosylation on the heparin-binding capability of boar and stallion seminal plasma proteins.},
  author={Juan J Calvete and M. Reinert and Libia Sanz and Edda T{\"o}pfer-Petersen},
  journal={Journal of chromatography. A},
  year={1995},
  volume={711 1},
  pages={167-73}
}
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-1 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… CONTINUE READING

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