Are the bonds between histone fraction and DNA of different strengths?

1980 ◽  
Vol 90 (2) ◽  
pp. 1058-1060 ◽  
Author(s):  
V. D. Paponov ◽  
P. S. Gromov ◽  
V. V. Rupasov
Keyword(s):  
Histone Fraction

scholarly journals A method for the selective extraction of histone fractions f2(a)1 and f2(a)2 from calf thymus deoxyribonucleoprotein at pH7

1967 ◽  
Vol 105 (2) ◽  
pp. 611-614 ◽  
Author(s):  
E W Johns
Keyword(s):  
Acid Solution ◽  
Selective Extraction ◽  
New Method ◽  
Guanidinium Chloride ◽  
Histone Fraction ◽  
Acetone Precipitation ◽  
Calf Thymus

1. A new method has been developed for the specific extraction of histone fraction f2(a) from calf thymus deoxyribonucleoprotein at pH7 by using a mixture of ethanol and guanidinium chloride. 2. Fraction f2(a) has been separated into the subfractions f2(a)1 and f2(a)2 by acetone precipitation from acid solution, and at pH7. 3. Modifications of existing electrophoretic methods are described that enable these fractions to be more easily characterized.

scholarly journals The stepwise removal of histones from chicken erythrocyte nucleoprotein

1968 ◽  
Vol 107 (2) ◽  
pp. 207-215 ◽  
Author(s):  
K. Murray ◽  
G. Vidali ◽  
J. M. Neelin
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Chicken Erythrocyte ◽  
Histone Fraction ◽  
Buffer Solutions ◽  
Avian Erythrocytes ◽  
Zone Electrophoresis ◽  
Exclusion Chromatography ◽  
Starch Gels

1. A fractionation of chicken erythrocyte histones was achieved simultaneously with their extraction from saline-washed nuclei by stepwise titrations to progressively lower pH values. 2. Different acids and dilute buffer solutions of comparable pH behaved similarly in stepwise extractions of histones. 3. The histone preparations so obtained were characterized by their amino acid composition and behaviour on zone electrophoresis in starch gels. 4. The fractionation by titration was quite sharp at appropriate pH ranges, and the histone fraction that is apparently unique to avian erythrocytes was obtained without contamination by other histone fractions. 5. Histones prepared by stepwise titration were fractionated further by cation-exchange and exclusion chromatography. The chromatographic behaviour and amino acid composition of the components permitted comparison with histones prepared by other methods. 6. Histone fraction IIb was resolved into its subfractions IIb1 and IIb2 by exclusion chromatography on Bio-Gel P-60. 7. Histone fractions III and IV, previously reported to be absent from chicken erythrocyte nuclei, were found in extracts made at pH1.

scholarly journals Studies on the primary structure of chicken erythrocyte histone fraction V

1971 ◽  
Vol 124 (2) ◽  
pp. 319-325 ◽  
Author(s):  
P. J. Greenaway
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Sequence Data ◽  
Acid Extraction ◽  
Chicken Erythrocyte ◽  
Histone Fraction

Histone fraction V was prepared by selective acid extraction from chicken erythrocyte nuclei. Amino acid sequence studies on the tryptic and thermolytic peptides are reported. Only a limited amount of overlapping sequence data was obtained.

scholarly journals The synthesis and decay of histone fractions and of deoxyribonucleic acid in the developing avian brain

1971 ◽  
Vol 123 (3) ◽  
pp. 465-469 ◽  
Author(s):  
Stephen C. Bondy
Keyword(s):  
Half Life ◽  
Deoxyribonucleic Acid ◽  
Decay Curve ◽  
Similar Rate ◽  
Avian Brain ◽  
Short Term ◽  
Histone Fraction ◽  
Histone Protein ◽  
Histone Proteins ◽  
Wide Range

1. The turnover of cerebral histones and DNA after injection of [4,5-3H]leucine or [methyl-3-3H]thymidine, respectively, was studied in the developing chick. 2. Chromatin was prepared from chick nuclei that had been purified by centrifugation through 1.9m-sucrose. 3. Nuclear proteins were fractionated into three major histone classes, F1 (lysine-rich), F2(b) (slightly lysine-rich) and [F3+F2(a)] (arginine-rich), and a non-histone protein residue. 4. The proportions of the histone classes remained constant throughout the period of development studied. 5. All histone fractions decayed at a similar rate, initially with a half-life of around 5 days, later with a half-life of 19 days. 6. Non-histone proteins from chromatin decayed in a heterogeneous manner with a wide range of half-lives. 7. Short-term labelling studies showed that all histone fractions were synthesized at the same rate. 8. Some non-histone proteins were very rapidly synthesized relative to histones. 9. DNA had a longer half-life than any histone fraction studied. A biphasic exponential decay curve with half-lives of 23 and 50 days was found. 10. It was concluded that the turnover of histones can occur independently of that of DNA and that different histone classes have similar rates of synthesis and decay.

The basic proteins of cell nuclei

1951 ◽  
Vol 235 (630) ◽  
pp. 565-595 ◽  
Keyword(s):  
Chemical Composition ◽  
Detailed Examination ◽  
Cell Nuclei ◽  
Constant Composition ◽  
Histone Fraction ◽  
Normal Cells ◽  
Basic Proteins ◽  
Cell Specificity ◽  
Composition Characteristic ◽  
Species Specific

Cell nuclei have been isolated from various types of tissues. Evidence is presented which indicates that no appreciable loss of their major components occurs during isolation. Nuclei from normal cells of a particular type possess a constant composition characteristic of that type. The basic proteins extracted from such nuclei are not homogeneous. When they are of the histone type they can be separated into two parts conveniently described as a main histone and a subsidiary histone fraction respectively. A subsidiary product has also been obtained from protamins. A study of the chemical composition of the main histones and the protamins has shown that some of these are unquestionably species-specific. The phenomenon of cell specificity of these basic proteins has also been established in a number of instances. One case of cell specificity has also been found among the subsidiary histones. The difficulty of purification has prevented the detailed examination of others. The possible physiological significance of cell specificity of the basic proteins of cell nuclei is discussed.

scholarly journals Histone acetylation and hormone action. Early effects of oestradiol-17β on histone acetylation in rat uterus

1972 ◽  
Vol 130 (3) ◽  
pp. 663-669 ◽  
Author(s):  
P. R. Libby
Keyword(s):  
Histone Acetylation ◽  
Actinomycin D ◽  
Target Tissue ◽  
Not Given ◽  
Rat Uterus ◽  
Histone Fraction ◽  
Immature Rat ◽  
Chromatin Proteins ◽  
Early Effects ◽  
Stimulation Of

The effect of oestradiol treatment on the acetylation of histones of the immature rat uterus has been studied. A 10μg dose of oestradiol causes a 70% increase at 5min and a 140% increase at 10min after administration in the labelling of the histone fraction F2+F3. No effect of oestradiol is seen on the labelling of histones F1 or acidic non-histone chromatin proteins. The oestradiol stimulation is seen in animals pretreated with either cycloheximide or actinomycin D. The stimulation of labelling caused by oestradiol is completely abolished by pretreatment of the animals with the anti-oestrogen, nafoxidine. The stimulation is given by lower doses of oestradiol, by stilboestrol and oestriol, but is not given by testosterone. These results suggest that stimulation of histone acetylation in the uterus is the earliest known effect of the hormone on its target tissue.

Specific Toxicity of Histone Fraction F2C against TLX5 Lymphoma Ascites Cells in vitro

Nature ◽  
1970 ◽  
Vol 228 (5277) ◽  
pp. 1201-1202 ◽  
Author(s):  
E. W. JOHNS ◽  
T. A. CONNORS
Keyword(s):  
Histone Fraction

Comparison of the histones from fish erythrocytes

1977 ◽  
Vol 55 (12) ◽  
pp. 1220-1227 ◽  
Author(s):  
Brian L. A. Miki ◽  
James M. Neelin
Keyword(s):  
Cation Exchange ◽  
Polyacrylamide Gel Electrophoresis ◽  
Exchange Chromatography ◽  
White Sucker ◽  
Cation Exchange Chromatography ◽  
Apparent Absence ◽  
Histone Fraction ◽  
Functional Homology ◽  
Diverse Species ◽  
Exclusion Chromatography

Because of contentions concerning the generality of cell-specific histone 5 (H5) in nucleated erythrocytes of species other than birds, the erythrocyte histones of carp, trout, perch, black crappie, and white sucker were studied under conditions which minimize proteolysis. All were examined by polyacrylamide gel electrophoresis, and histone 1 (H1) and H5 were purified by cation-exchange chromatography on Amberlite CG-50 and by exclusion chromatography through BioGel P60.A protein homologous to H5 could be isolated and identified from the mature erythrocytes of carp, trout, perch, and black crappie but not from white sucker. The relative amounts of H5 differed extensively and inversely in proportion to H1, implying some functional homology between these proteins. The extremely variable levels of H5, including its apparent absence from one species, suggests that typical H5 is not essential to the function or development of nucleated erythrocytes.Although H1 is the most divergent histone fraction, H5 is also highly variable. Fish erythrocyte H5 differs from avian H5 in relative electrophoretic mobility, ease of elution from Amberlite CG-50 cation-exchange columns, and amino acid composition. H5's from fish tend to have more threonine but less serine, arginine, glutamic acid, and histidine than avian H5's. Fish H5's are more diverse than avian H5's and resemble the H5 homologues from other extremely diverse species; thus avian H5 may be an extreme in specialization of an H1 subfraction.

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