Aggregated forms of heparin-binding and non-heparin-binding proteins of boar seminal plasma and their binding properties
Jazyk angličtina Země Česko Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
PubMed
10730888
Knihovny.cz E-zdroje
- MeSH
- chondroitinsulfáty metabolismus MeSH
- chromatografie afinitní MeSH
- heparin metabolismus MeSH
- kapacitace spermií MeSH
- kyselina hyaluronová metabolismus MeSH
- makromolekulární látky MeSH
- molekulová hmotnost MeSH
- polysacharidy metabolismus MeSH
- prasata metabolismus MeSH
- proteiny izolace a purifikace metabolismus MeSH
- sekvenční analýza proteinů MeSH
- síran dextranu metabolismus MeSH
- sperma chemie MeSH
- tělesné tekutiny chemie MeSH
- vazba proteinů MeSH
- vysokoúčinná kapalinová chromatografie MeSH
- zona pellucida metabolismus MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- chondroitinsulfáty MeSH
- fucoidan MeSH Prohlížeč
- heparin MeSH
- kyselina hyaluronová MeSH
- makromolekulární látky MeSH
- polysacharidy MeSH
- proteiny MeSH
- síran dextranu MeSH
Boar seminal plasma proteins were separated by affinity chromatography on immobilized heparin into two portions: heparin-binding (H+) and non-heparin-binding (H-) proteins. Gel chromatography of the H+ portion yielded four main protein fractions of >150, 45, 30 and 20 kDa, while that of the H- portion resulted in the separation into three main protein fractions of >150, 30 and 20 kDa. HPLC analysis and N-terminal sequencing used to characterize the composition of the protein fractions obtained by gel chromatography revealed that all consisted of low (12-16 kDa) molecular weight components: the H+ fraction consisted of DQH sperm protein, AQN and AWN spermadhesins whereas the H- fraction consisted of PSPI and PSPII spermadhesins. The high molecular weight values of fractions obtained by gel chromatography thus suggest that the proteins are present in boar seminal plasma in the form of aggregates. Interactions of individual boar seminal plasma proteins and their aggregates present in the H+ and H- fractions with acid polysaccharides were estimated.
Effect of Seminal Plasma Protein Fractions on Stallion Sperm Cryopreservation
