Proteinase inhibitors in aggregated forms of boar seminal plasma proteins
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12957306
DOI
10.1016/s0141-8130(03)00043-6
PII: S0141813003000436
Knihovny.cz E-zdroje
- MeSH
- gelová chromatografie MeSH
- inhibitory proteas chemie izolace a purifikace farmakologie MeSH
- molekulární sekvence - údaje MeSH
- molekulová hmotnost MeSH
- sekvence aminokyselin MeSH
- sperma chemie MeSH
- Sus scrofa * MeSH
- vysokoúčinná kapalinová chromatografie MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- inhibitory proteas MeSH
Boar seminal plasma proteins were separated by gel chromatography on Sephadex G-75 into five fractions (I-V). Serine proteinase inhibitors were found mainly in the protein fraction with relative molecular weight 5-25kDa. Small amounts of these inhibitors were also found in the high molecular weight protein fraction (M(r)>100kDa). The protein fraction containing most of the proteinase inhibitory activity was further separated by RP HPLC. Isolated proteins were characterized by SDS electrophoresis and immunoblotting, N-terminal amino acid sequencing and by determination of the proteinase inhibitory activity. In the fraction containing proteinase inhibitors, also beta-microseminoprotein (beta-MSP), AQN 1 and lactoferrin were identified. The possible existence of complexes of protein components in the fraction with relative molecular weight 5-25kDa was studied in detail using gel chromatographic separation on Sephadex G-50. A part of proteinase inhibitors with M(r) 8kDa was eluted together with AQN 1 spermadhesin. An interaction of isolated spermadhesin AQN 1 and proteinase inhibitor was shown.
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