Abstract
Two major glycoproteins, designated PSP-I and PSP-II, were purified from porcine seminal plasma by ammonium sulfate fractionation, CM-cellulose chromatography, gel filtration on Sephadex G-75 (superfine), and reverse phase high performance liquid chromatography. These two proteins exist in several forms differing mainly in the carbohydrate moiety. The complete amino acid sequence of PSP-I has been determined by automated Edman degradation of peptides generated by proteolytic digestion and cyanogen bromide cleavage. The protein is 109 residues long and has a single glycosylation site at the asparagine residue at position 47. In addition, the N-terminal sequence of PSP-II has also been determined. PSP-I is a unique protein; a sequence homology search using the protein data base did not reveal any significant homology with other proteins. PSP-II shares 50% sequence homology with a family of zona pellucida-binding glycoproteins at the N-terminus.
Original language | English (US) |
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Pages (from-to) | 352-359 |
Number of pages | 8 |
Journal | Archives of Biochemistry and Biophysics |
Volume | 295 |
Issue number | 2 |
DOIs | |
State | Published - Jun 1992 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology