Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities.

@article{Calvete1995AminoAS,
  title={Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities.},
  author={Juan J Calvete and Karlheinz Mann and Wolfgang Schaefer and Libia Sanz and M. Reinert and S Nessau and Manfred Raida and Edda T{\"o}pfer-Petersen},
  journal={The Biochemical journal},
  year={1995},
  volume={310 ( Pt 2)},
  pages={615-22}
}
We report the complete amino acid sequence of HSP-1, a major protein isolated from stallion seminal plasma or acid extracts of ejaculated spermatozoa. The protein consists of 121 amino acids organized in two types of homologous repeats arranged in the pattern AA'BB'. Each of the 13-15-residue A-type repeats contains two O-linked oligosaccharide chains. The B-type repeats span 44-47 amino acids each, are not glycosylated, and have the consensus pattern of the gelatin-binding fibronectin type-II… CONTINUE READING
29 Citations
2 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 29 extracted citations

References

Publications referenced by this paper.
Showing 1-2 of 2 references

Proteins of Seminal Plasma

  • S. Shivaji, Scheit, K.-H, P. M. Bhargava
  • 1990

Elements of Mammalian Fertilization (Wassarman

  • H. M. Florman, D. F. Babcock
  • P. M., ed.),
  • 1984

Similar Papers

Loading similar papers…