Characterization of peptide proteinase inhibitors isolated from boar seminal plasma

0191602 - UMG-J 20033106 RIV CZ eng G - Konferenční sborník (zahraniční konf.)
Jelínková, Petra - Tichá, M. - Jonáková, Věra - Slaninová, J. (ed.)
Characterization of peptide proteinase inhibitors isolated from boar seminal plasma.
Praha: Visit, s.r.o., 2003. 128 s. volume 6. ISBN 80-86241-20-3. Collection Symposium Series : Biologically Active Peptides.
[Biologically Active Peptides /8./. Praha (CZ), 23.04.2003-25.04.2003]
Grant CEP: GA ČR GA303/02/0433; GA ČR GP303/02/P069; GA MZd NJ7463
Výzkumný záměr: CEZ:MSM 113100001
Klíčová slova: proteinase inhibitors, aggregated forms, boar seminal plasma
Kód oboru RIV: CE - Biochemie

Most of proteins of boar seminal plasma are present in this medium under physiological conditions in the form of aggregates and not of monomers. In the present communication we have shown that not only spermadhesins, but also proteinase inhibitors participate in the formation of associated complexes. Proteinase inhibitors were found after gel chromatographic separation mainly in the fraction with the lowest relative molecular mass. Two different types of serine proteinase inhibitors were isolated from boar seminal plasma ů (i) glycosylated inhibitor with Mr 12 kDa, (ii) non-glycosylated sperm-associated acrosin inhibitor with Mr 8 kDa, and a new type of low molecular weight protein that is probably composed of two subunits coupled by the -S-S- bridge. The proteinase inhibitor with Mr 8 kDa was proved to form a heterodimer with AQN 1 spermadhesin under physiological conditions, whereas inhibitor with Mr 12 kDa forms homodimers.
Trvalý link: http://hdl.handle.net/11104/0087342