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 |
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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. |
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ISSN: | 1570-0232 1873-376X |
DOI: | 10.1016/S0378-4347(01)00480-7 |