Isolation of non-heparin-binding and heparin-binding proteins of boar prostate
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12013220
DOI
10.1016/s0378-4347(01)00480-7
PII: S0378434701004807
Knihovny.cz E-zdroje
- MeSH
- chromatografie afinitní metody MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- heparin metabolismus MeSH
- kationické antimikrobiální peptidy MeSH
- krevní proteiny izolace a purifikace metabolismus MeSH
- prasata MeSH
- prostata metabolismus MeSH
- transportní proteiny izolace a purifikace metabolismus MeSH
- vysokoúčinná kapalinová chromatografie metody MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- AZU1 protein, human MeSH Prohlížeč
- heparin MeSH
- kationické antimikrobiální peptidy MeSH
- krevní proteiny MeSH
- transportní proteiny 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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