Proteinase inhibitors in aggregated forms of boar seminal plasma proteins
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12957306
DOI
10.1016/s0141-8130(03)00043-6
PII: S0141813003000436
Knihovny.cz E-resources
- MeSH
- Chromatography, Gel MeSH
- Protease Inhibitors chemistry isolation & purification pharmacology MeSH
- Molecular Sequence Data MeSH
- Molecular Weight MeSH
- Amino Acid Sequence MeSH
- Semen chemistry MeSH
- Sus scrofa * MeSH
- Chromatography, High Pressure Liquid MeSH
- Animals MeSH
- Check Tag
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Protease Inhibitors 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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