[Characteristic of acid soluble group of DNA-binding proteins of cereals]
2007
Spiridovich, E.V. | Chizhik, V.V. | Goncharova, L.V.,National Academy of Sciences, Minsk (Belarus). Central Botanical Garden
Research results of studies of heterogeneity and specificity of DNA-binding proteins of various cereals species were presented. Research results showed that 4 fractions of H1 histons evolved from secalotriticum germs and 5 fractions of H1 histone obtained in the process of histons division of rye (Secale cereale L.) of Verasen variety in the system acetic acid / urea after the further distillation in the second targeting divided into the additional subzones. Electrophoregram of rye of Verasen variery showed the presence of 10 sub-zones. Secalotriticum S206 in the conditions of two-dimensional division showed 12 sub-fractions that proved the variability of H1 histone and its possible application as the protein marker on the level of family or species of higher plant. The protein (polypeptide) heterogeneity of total preparation of nuclei proteins of single representatives of Gramineae family and density composition of HMG-proteins of nuclei of winter rye was determined. Two-dimensional electrophoresis in polyacrylamide gel proved the histones heterogeneity within limits of cereals family (rye, wheat and secalotriticum) and showed the species specificity of cereals family according to the observed index, first of all according to the H1 histons subfractions number. HMG-proteins were presented in rye nuclei alongside with histons that required their division by means of two-dimensional electrophoresis with the further isolation of aminoacid composition
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