Isolation of non-heparin-binding and heparin-binding proteins of boar prostate
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12013220
DOI
10.1016/s0378-4347(01)00480-7
PII: S0378434701004807
Knihovny.cz E-resources
- MeSH
- Chromatography, Affinity methods MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Heparin metabolism MeSH
- Antimicrobial Cationic Peptides MeSH
- Blood Proteins isolation & purification metabolism MeSH
- Swine MeSH
- Prostate metabolism MeSH
- Carrier Proteins isolation & purification metabolism MeSH
- Chromatography, High Pressure Liquid methods MeSH
- Animals MeSH
- Check Tag
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- AZU1 protein, human MeSH Browser
- Heparin MeSH
- Antimicrobial Cationic Peptides MeSH
- Blood Proteins MeSH
- Carrier Proteins MeSH
Proteins of boar prostate secretion were separated by affinity chromatography on heparin-polyacrylamide to non-heparin-binding (H) and heparin-binding (H+) protein fractions. H- and H+ fractions were then subjected to RP HPLC. Elution profiles of H-and H+ fractions of prostate secretion were compared with those of seminal plasma and the amounts of corresponding proteins were compared. Besides, the isolated proteins were characterized by SDS-PAGE. In the H- fraction of prostate secretion, PSP I and PSP II spermadhesins and in the H+ fraction AQN 2 and AWN 1 spermadhesins were found in substantially lower amounts than in seminal plasma. On the contrary, beta-microseminoprotein was identified in abundant amounts both in H- and H+ fractions of boar prostate secretion. AQN 2 and AWN 1 spermadhesins were proved by their antibodies. Some seminal plasma proteins originating mainly in seminal vesicles could also be secreted by the prostatic gland. beta-Microseminoprotein was found to be produced mainly by the prostate.
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