Počet záznamů: 1
Biochemical and binding characteristics of boar epididymal fluid proteins
0353966 - BTO-N 2012 RIV NL eng J - Článek v odborném periodiku
Maňásková-Postlerová, Pavla - Davidová, Nina - Jonáková, Věra
Biochemical and binding characteristics of boar epididymal fluid proteins.
Journal of Chromatography B-Analytical Technologies in the Biomedical and Life Sciences. Roč. 879, č. 1 (2011), s. 100-106 ISSN 1570-0232
Grant CEP: GA ČR(CZ) GA303/09/1285; GA MŠk(CZ) 1M06011; GA ČR(CZ) GD523/08/H064
Výzkumný záměr: CEZ:AV0Z50520701
Klíčová slova: epididymal proteins * RP HPLC * biotin-labeled ligands
Kód oboru RIV: CE - Biochemie
Impakt faktor: 2.888, rok: 2011
Proteins and glycoproteins of boar epididymal fluid may be adsorbed on the sperm surface and participate in the sperm maturation, in sperm capacitation, gamete recognition, binding and fusion. Boar epididymal fluid proteins were separated by size exclusion chromatography and by RP-HPLC. The fractions were characterized by SDS-PAGE and proteins were transfered to nitrocellulose membranes and tested for the interaction with biotin-labeled ligands: glycoproteins of zona pellucida (ZP), hyaluronic acid and heparin. Changes in the interaction of epididymal sperm were studied by ELBA. The affinity of epididymal proteins (12-17 kDa, 23 kDa) to heparin and hyaluronic acid suggests their binding ability to oviductal proteoglycans. Epididymal proteins of 12-18 kDa interacted with ZP glycoproteins. We identified Crisp3-like protein. We showed the ability of epididymal fluid fractions to change the interaction of the epididymal sperm surface with ZP glycoproteins, hyaluronic acid and heparin.
Trvalý link: http://hdl.handle.net/11104/0193066