Mammalian fertilization is a sequence of unique and fascinating events, during which seminal proteins are of crucial role. In case of bull (Bos taurus), proteins of seminal plasma (BSP), especially its major component PDC-109, are known to be in aggregated forms, but little is known about mechanism of forming aggregates and their biological function. In present thesis we discovered some interesting properties of PDC-109 and BSP proteins. We found that concentration of these proteins influences their aggregation state significantly, which can be of great biological importance. Separation of seminal proteins by size exclusion chromatography revealed three main fractions denoted I, II and III, with apparent molecular weights of Mr > 150 000, Mr = 30 000 and Mr = 13 000, respectively. In case of PDC-109, molecular weights of theese fractions were retained even after purification procedure, which implies very stable interactions in forming of aggregates. In addition, there was a difference in distribution of PDC-109 glycoforms among fractions, which can be related to the fact, that theese fractions have different sperm membrane binding patterns as we determined by fluorescence microscopy. However, further experiments are needed for better understanding this issue.
| Identifer | oai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:313228 |
| Date | January 2012 |
| Creators | Boháček, Hanuš |
| Contributors | Liberda, Jiří, Hýsková, Veronika |
| Source Sets | Czech ETDs |
| Language | Czech |
| Detected Language | English |
| Type | info:eu-repo/semantics/masterThesis |
| Rights | info:eu-repo/semantics/restrictedAccess |
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