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The aim of this work was to determine the activity of the akrosin inhibitor on the basis of depressing the tripsin activity of polar fox (Alopex lagopus) semen and to follow the changes that affect these properties throughout the whole reproductive season. Additionally, the molecular forms of the inhibitor were electrophoretically separated. The research covered 126 ejaculates obtained manually seven times from 18 polar foxes (at intervals of 10-12 days). The highest inhibitor activity was observed in the seminal plasma from the ejaculates obtained in the first sample, the lowest results were characteristic of the fifth sample. The lowest activity of the akrosin inhibitor, determined on the basis of depressing the tripsin activity, indicates either the weakest protection of the semen proteins along with the whole reproductive system from the influence of the akrosin devoid of damaged acrosomes or the already initiated process of proteolysis.
An attempt was made to use a modified 2-D PAGE technique to analyze seminal plasma proteins and their polymorphisms in relation to boar age and season. The 2-D PAGE analysis of seminal plasma proteins was performed using a buffer pH gradient of 3 to 10. Modifications to the 2-D PAGE procedure included substituting mercaptoethanol (ME) with dithiothreitol (DTT) and the use of a specific reagent assay (Plus One 2-D Clean-Up Kit, Amersham Biosciences), which markedly improved the resolution of the electrophoregrams. Polymorphisms by polypeptide mapping of boar seminal plasma were dependent on the animal age and season. Furthermore, the amount of polypeptides detected in the seminal plasma was significantly lower in 12 month-old boars compared with 3 year-olds. Additionally, the seminal plasma polypeptides were markedly lower in the summer than in the autumn. The results of the study showed that mapping seminal plasma proteins may be used as a marker for the secretor activity of boar accessory sex glands, and as a selection criterion for male reproduction.
The seminal plasma of teleost fish contains a species-specific system of proteins with anti-trypsin activity. Serine proteinase inhibitors are one of the main proteins of fish seminal plasma and their electrophoretic pattern is similar to blood plasma. Anti-trypsin activity correlates with protein and sperm concentration. To date one of the proteinase inhibitors of seminal plasma of common carp and rainbow trout has been identified. It belongs to the serpin family and is similar to α₁ -antiproteinase. A characteristic feature of this inhibitor is the ability to form an irreversible complex with serine proteinases. Serine proteinase inhibitors of fish seminal plasma may participate in the protection of reproductive tissue and spermatozoa from proteolytic attack.
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