Isolation of non-heparin-binding and heparin-binding proteins of boar prostate

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...

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Veröffentlicht in:Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Analytical technologies in the biomedical and life sciences, 2002-04, Vol.770 (1), p.137-143
Hauptverfasser: Maňásková, Pavla, Liberda, Jiřı́, Tichá, Marie, Jonáková, Věra
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Sprache:eng
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Zusammenfassung: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, β-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. β-Microseminoprotein was found to be produced mainly by the prostate.
ISSN:1570-0232
1873-376X
DOI:10.1016/S0378-4347(01)00480-7