The subfraction composition of lysine-rich histone has been studied with the aid of polyacrylamide gel electrophoresis. The subfraction compositions of the histone F1 of several tissues from the chicken, pigeon, and titmouse have been compared. The histone F1 from the tissues investigated consists of four or five subfractions of similar number and electrophoretic mobility (1, 1a, 2, 3, and 4). In the different avian species each subfraction varied its mobility independently of the others. The chicken tissues investigated can be divided into two classes, depending on the relative concentration of subfractions 2 and 3 (A and B): Class A (subfraction 2 is smaller than 3) includes the brain, liver, skeletal muscle, heart, muscular layer of the stomach, and pancreas, and class B (subfraction 2 is larger than 3) includes the intestinal mucosa, thymus, and testes, as well as the liver, heart, and pancreas from a 21-day embryo. Such a division of the tissues corresponds to the varying rate of their cellular renewal. In a parallel examination of the relative concentrations of the individual subfractions in the same tissues from the three avian species it has been found that the relative concentration of subfractions 3 and 2 is increased in the skeletal muscles, heart, brain, and liver, that subfraction 2 is increased in the intestinal mucosa, that subfractions 4 and 3 are increased in the pancreas, and that subfractions 1, 1a, and 4 are increased in the erythrocytes. The results obtained may be interpreted as a consequence of some relationship between the subfraction composition of histone F1 and the type of tissue of the source.

Amino Acid Sequence↗

PubMedDate not supplied

[Histones of some invertebrates].

Explore the source record for details and available documents.

Animals↗

PubMedDate not supplied

Determination of the fraction of histone-free phosphate groups in certain chromatins.

Explore the source record for details and available documents.

Animals↗

PubMedDate not supplied

[Dansylated amino acid separation by polyacrylamide gel electrophoresis].

The paper describes a method for separation of dansylated amino acids by polyacrylamide gel electrophoresis. The methods allows a simultaneous analysis of 20-30 samples. The sensitivity of the method is 1 x 10(-9)-1 x 10(-10) M amino acid. The method permits separation of all amino acids formed during acid hydrolysis of proteins except for two pairs: Ile, Phe and Val, Asp.

Amino Acids↗

PubMedDate not supplied

[Structural characteristics of lysine-rich histone from the sperm of a mollusk Anodonta piscinalis].

Sperm of freshwater bivalve mollusk Anodonta piscinalis was found to contain two fractions of lysine-rich histone: somatic histone H1 and sperm-specific protamine-like histone, named Hp. A detailed analysis of H1 and Hp structure was carried out by means of N-bromosuccinimide, chymotrypsin and pepsin cleavage followed by determination of the lysine residue number, positive charge and molecular length of obtained fragments by the method of incomplete succinylation. It has been shown, that Anodonta histone H1, like the avian histone H5, contains 3 tyrosine residues in the central hydrophobic domain of the molecule. Histone Hp contains 5 tyrosine residues, 3 of which are localized in the hydrophobic domain, while the rest two--in the COOH-terminal part of the molecule, characterized by a strong positive charge. Such unusual disposition of tyrosine residues in the lysine-rich histone has been found for the first time. All the regions of histone Hp molecule contain a great number of arginine residues. The only phenylalanine residue is localised approximately in the middle of the polypeptide chain for both H1 and Hp molecules. On the basis of structure homology between histones H1 and Hp the origin of Hp from H1 in the course of evolution is proposed.

Amino Acid Sequence↗

PubMedDate not supplied

[Evolutionary interrelationship of histones H1 and H5 in vertebrates].

Lysine-rich histones of some amphibians and fishes were studied. Electrophoretically purified subfractions were cleaved at residues of tyrosine, methionine, aspartic acid and phenylalanine. The fragments thus obtained were investigated by the method of incomplete succinylation which permitted us to determine the number of lysine residues, positive charge in acid conditions and molecular lengths of polypeptides. It was found that in anura and shark the fraction H1a resembled the histone 5 of birds in its N-terminal half part of the molecule. However this fraction proved to be non-tissue-specific. Other histone 1 fractions characteristic for vertebrates were represented in the present study by molecular variant H1s which was different from H1a fraction by the number and position of tyrosine, methionine and aspartic acid residues. The erythrocyte-specific fraction of the lysine rich histone was found in the following families of fishes: Salmonidae, Percidae and Cyprinidae. A high degree of homology in the structure of N-terminal half of H1s and histone 5 of fishes has been observed. On the basis of these results we propose a hypothesis of the independent origin of the avian and fish H5 from different fractions of H1.

Amino Acid Sequence↗

PubMedDate not supplied

[Histone H1 of reptiles, homologous to histone H5 of birds].

Lysine-rich histone H1 of animals from three reptilian orders was studied. Electrophoretically pure H1 histone subfractions were cleaved at residues of tyrosine, methionine, aspartic acid and phenylalanine. The fragments obtained were studied by modified method of incomplete succinylation which permitted to determine the number of lysine residues, the positive charge and molecular length of polypeptides. The structural homology between the fastest reptilia H1 subfraction and avian H5 histone has been shown.

Amino Acid Sequence↗

PubMedDate not supplied

[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.

Bromosuccinimide↗