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Glycoprotein profile of human ejaculate as a marker of its quality
Pavlová, Hana ; Postlerová, Pavla (advisor) ; Krejčová, Tereza (referee)
Glycoproteins are an indispensable component of the sperm glycocalyx. They arise through the process of co-translational or post-translational modification, so-called glycosylation, during which carbohydrate chains are attached to a peptide chain. Glycoproteins are involved in reproductive processes and their presence is often key to successful fertilization. The degree of glycosylation of glycoproteins is highly variable and is determined by the representation of carbohydrate units in glycans. It has already been found that the degree of glycosylation can be related to the fertility of an individual. The diploma thesis is focused on the comparison of the representation of terminal saccharides, sialic acid and fucose, in the glycoproteins of sperm and seminal plasma of patients with normal and abnormal ejaculate parameters. The total rate of sialylation and fucosylation in the seminal plasma was determined, as well as the rate of sialylation and fucosylation of specifically detected glycoproteins of sperm and seminal plasma. A significant difference was noted only in the detection of total fucosylation of seminal plasma glycoproteins. However, subsequent correlation tests revealed important relationship between the degree of sialylation and fucosylation of glycoproteins and ejaculate parameters,...
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Aggregation of bull seminal plasma protein
Boháček, Hanuš ; Liberda, Jiří (advisor) ; Hýsková, Veronika (referee)
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.
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Aggregation of bull seminal plasma protein
Boháček, Hanuš ; Liberda, Jiří (advisor) ; Hýsková, Veronika (referee)
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.
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