[Quantitative changes in histones during the formation of structures characteristic of the male pronucleus in mammalian spermatozoa in vitro]. / Kolichestvennye izmeneniia gistonov pri obrazovanii v spermatozoidakh mlekopitaiushchikh in vitro struktur, svoistvennykh muzhskomu pronukleusu.

Treatment of bull spermatozoa with DDC--Na/dithiothreitol results in the swelling and decondensation of nuclear chromatin. The structures formed at the final stages of decondensation are morphologically similar to the male pronucleus. Cytophotometric analysis has shown that decondensation of chromatin in the gametes in followed by quantitative changes of basic nuclear proteins. In partly--decondensed sperm nuclei the intensity of histone staining increases as a result of the appearance of extra reactive groups. In fully decondensed nuclei there remain only 54% of histones of the original haploid level. Nucleoproteins revealed in the sperm with fully dispersed chromatin must be histones of the somatic type.

[Glycoprotein complexes in bull seminal fluid diluted with yolk media]. / Glikoproteinni kompleksi v razredena s zhultuchni sredi semenna technost ot bitsi.

Electrophoresis on celogel and staining the bands with Schiff's agent were used to study the sugar fractions in the diluents Nagase Niva, Triladil, Leciphos and GH22L (after Kichev) as well as in bull semen diluted to a various extent with the same media. Using combined staining--sugars/proteins--it was found that all sugar fractions in both media and diluted semen were bound with proteins. These biocomplexes were found to lower their electrophoretic mobility with the rising values of dilution. Discussed is the possibility to use the conformation of sugar complexes in the working out of new cryoprotective media.