Literature DB >> 5533201

A study of calf thymus histone fraction F2(b) by gel filtration.

P A Edwards, K V Shooter.   

Abstract

The gel-filtration behaviour of calf thymus histone fraction F2(b) was studied at three different salt concentrations (0.01m-, 0.10m- and 1.00m-sodium chloride) and two different pH ranges (pH3-4 and pH6.7-7.1). Other histone fractions [F1, F2(a) and F3] were also utilized to assist interpretation of the data. It was found that the Stokes radius of histone fraction F2(b) was not significantly changed when the salt concentration was increased, implying that the aggregation of the individual histone molecules (Edwards & Shooter, 1969) resulted in only relatively minor changes in the hydrodynamic volume. Aggregation would appear to be due to the salting out of hydrophobic regions giving rise, in the aggregate, to a compact core of hydrophobic groups from which protrude the remaining basic parts of the molecule. Repulsion between charged groups on the basic regions of individual histone molecules would give the aggregate approximately spherical symmetry, the diameter of the aggregate approximating to the length of a single histone molecule.

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Year:  1970        PMID: 5533201      PMCID: PMC1179569          DOI: 10.1042/bj1200061

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  15 in total

1.  The molecular size and shape of the pancreatic proteases. II. Chymotrypsinogen.

Authors:  G W SCHWERT
Journal:  J Biol Chem       Date:  1951-06       Impact factor: 5.157

2.  Assymetry in the distribution of basic amino acid residues in the moderately lysine-rich histone F2b from calf thymus.

Authors:  L S Hnilica; H A Kappler; J J Jordan
Journal:  Experientia       Date:  1970-04-15

3.  Sedimentation equilibrium and other physicochemical studies on the lysine-rich fraction of calf thymus histones.

Authors:  A J Haydon; A R Peacocke
Journal:  Biochem J       Date:  1968-11       Impact factor: 3.857

4.  Ultracentrifuge tudies of histone fractions from calf thymus deoxyribonucleoprotein.

Authors:  P A Ewars; K V Sooter
Journal:  Biochem J       Date:  1969-09       Impact factor: 3.857

5.  Structural analysis of the glycine-rich, arginine-rich histone. 3. Sequence of the amino-terminal half of the molecule containing the modified lysine residues and the total sequence.

Authors:  Y Ogawa; G Quagliarotti; J Jordan; C W Taylor; W C Starbuck; H Busch
Journal:  J Biol Chem       Date:  1969-08-25       Impact factor: 5.157

6.  Studies on histones. 7. Preparative methods for histone fractions from calf thymus.

Authors:  E W Johns
Journal:  Biochem J       Date:  1964-07       Impact factor: 3.857

7.  On the estimation of the shape of macromolecules from sedimentation and viscosity measurements.

Authors:  J M Creeth; C G Knight
Journal:  Biochim Biophys Acta       Date:  1965-07-22

8.  The molecular weight of lysine-rich histone.

Authors:  D C Teller; J M Kinkade; R D Cole
Journal:  Biochem Biophys Res Commun       Date:  1965-09-22       Impact factor: 3.575

9.  Super-helical model for nucleohistone.

Authors:  J F Pardon; M H Wilkins; B M Richards
Journal:  Nature       Date:  1967-07-29       Impact factor: 49.962

10.  Calf and pea histone IV. II. The complete amino acid sequence of calf thymus histone IV; presence of epsilon-N-acetyllysine.

Authors:  R J DeLange; D M Fambrough; E L Smith; J Bonner
Journal:  J Biol Chem       Date:  1969-01-25       Impact factor: 5.157

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  1 in total

1.  A model for chromatin sub-structure incorporating symmetry considerations of histone oligomers.

Authors:  J E Hyde; I O Walker
Journal:  Nucleic Acids Res       Date:  1975-03       Impact factor: 16.971

  1 in total

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