[Molecular variants of histone H5 of linnet (Acanthis flammea)].

Five electrophoretic variants of H5 histone were detected in the population of linnet (Acanthis flammea). Using the method of incomplete succinilation the number of lysine residues, electrophoretic positive charge and molecular length were determined for some variants of H5 histone and for their fragments, obtained after treatment with n-bromosuccinimide and chymotrypsin. The difference in structure of H5 variants was found to be connected with the region, confined by the phenylalanine residue and the C-end of the molecule. The minimal difference in molecular length of fragments carrying the variable region was found to be 6 amino acids, two of them are basic. A series of "regular" fragments was detected after mild treatment with trypsin. The number of these fragments increased in parallel with the increase of histone length. In accordance with the scheme proposed, the difference in structure of linnet H5 variants is caused by insertion of the regular region consisting of tandem repeats (from 3 to 7 times) of the elementary hexapeptide.