Aggregated forms of bull seminal plasma proteins and their heparin-binding activity

0191692 - UMG-J 20033208 RIV CZ eng J - Journal Article
Jelínková, Petra - Ryšlavá, H. - Liberda, J. - Jonáková, Věra - Tichá, M.
Aggregated forms of bull seminal plasma proteins and their heparin-binding activity.
Collection of Czechoslovak Chemical Communications. Roč. 69, - (2004), s. 616-630. ISSN 0010-0765
R&D Projects: GA ČR GA303/02/0433; GA ČR GP303/02/P069; GA MZd NJ7463
Institutional research plan: CEZ:AV0Z5052915; CEZ:MSM 113100001
Keywords : bull seminal plasma proteins * heparin-binding proteins * aggregated forms of proteins
Subject RIV: CE - Biochemistry
Impact factor: 1.062, year: 2004

Heparin-binding activity of bull seminal plasma proteins was shown to be dependent on their aggregation state. Protein fraction interacting with immobilized heparin was characterized by large polydispersity in the region of relative molecular mass of 60 000 ů 100 000 while that not retained on the affinity carrier was present as aggregates with relative molecular mass >100 000. Components of heparin-binding and non-heparin-binding fractions were separated by RP HPLC and analyzed by SDS electrophoresis and N-terminal sequencing. Size exclusion chromatography of whole seminal plasma and heparin-binding proteins in the presence of D-fructose (as a component of seminal plasma) showed that the region of relative molecular masses of protein associated forms was shifted to lower values. An increase of heparin-binding activity of bull proteins, as determined by ELBA, correlates with a decrease of their aggregation state. The modulation of the aggregation state of bull proteins by seminal plasma components and by this way also their heparin-binding properties suggest possible mechanisms for capacitation mediated by these proteins.
Permanent Link: http://hdl.handle.net/11104/0087429