Proteinase inhibitors in aggregated forms of boar seminal plasma proteins.
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.
Jelínková
Petra
P
Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic. petraj@zeus.img.cas.cz
Manásková
Pavla
P
Tichá
Marie
M
Jonáková
Vera
V
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology; D012661:Semen / Q000737:chemistry*; D034421:Sus scrofa
D011480:Protease Inhibitors