Boar spermadhesin PSP-II: location of posttranslational modifications, heterodimer formation with PSP-I glycoforms and effect of dimerization on the ligand-binding capabilities of the subunits.

@article{Calvete1995BoarSP,
  title={Boar spermadhesin PSP-II: location of posttranslational modifications, heterodimer formation with PSP-I glycoforms and effect of dimerization on the ligand-binding capabilities of the subunits.},
  author={Juan J Calvete and Karlheinz Mann and Wolfgang Schaefer and Manfred Raida and Libia Sanz and Edda T{\"o}pfer-Petersen},
  journal={FEBS letters},
  year={1995},
  volume={365 2-3},
  pages={179-82}
}
Spermadhesin PSP-II was isolated from the non-heparin-binding fraction of boar seminal plasma; its disulphide bridge pattern, and the location of a single N-glycosylation site were established. PSP-II forms a heterodimer with specific N-glycoforms of PSP-I. Although both subunits possess heparin-binding capability, the PSP-I/PSP-II complex does not. The heterodimer contains binding sites for zona pellucida glycoproteins and soybean trypsin inhibitor located in the PSP-II subunit. However, the… CONTINUE READING
19 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 19 extracted citations

Similar Papers

Loading similar papers…