Aggregated forms of bull seminal plasma proteins and their heparin-binding activity
1.
SYSNO ASEP
0191692
Document Type
J - Journal Article
R&D Document Type
Journal Article
Subsidiary J
Ostatní články
Title
Aggregated forms of bull seminal plasma proteins and their heparin-binding activity
Author(s)
Jelínková, Petra (UMG-J) Ryšlavá, H. (CZ) Liberda, J. (CZ) Jonáková, Věra (UMG-J) Tichá, M. (CZ)
Source Title
Collection of Czechoslovak Chemical Communications. - : Ústav organické chemie a biochemie AV ČR, v. v. i.
- ISSN 0010-0765
Roč. 69, - (2004), s. 616-630
Number of pages
15 s.
Language
eng - English
Country
CZ - Czech Republic
Keywords
bull seminal plasma proteins ; heparin-binding proteins ; aggregated forms of proteins
Subject RIV
CE - Biochemistry
R&D Projects
GA303/02/0433 GA ČR - Czech Science Foundation (CSF)
GP303/02/P069 GA ČR - Czech Science Foundation (CSF)
NJ7463 GA MZd - Ministry of Health (MZ)
CEZ
AV0Z5052915 - UMG-J
MSM 113100001
Annotation
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.
