Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1970 Nov;120(1):61–66. doi: 10.1042/bj1200061

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

P A Edwards 1, K V Shooter 1
PMCID: PMC1179569  PMID: 5533201

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.

Full text

PDF
61

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ACKERS G. K. MOLECULAR EXCLUSION AND RESTRICTED DIFFUSION PROCESSES IN MOLECULAR-SIEVE CHROMATOGRAPHY. Biochemistry. 1964 May;3:723–730. doi: 10.1021/bi00893a021. [DOI] [PubMed] [Google Scholar]
  2. BERNS K. I., THOMAS C. A., Jr ISOLATION OF HIGH MOLECULAR WEIGHT DNA FROM HEMOPHILUS INFLUENZAE. J Mol Biol. 1965 Mar;11:476–490. doi: 10.1016/s0022-2836(65)80004-3. [DOI] [PubMed] [Google Scholar]
  3. Creeth J. M., Knight C. G. On the estimation of the shape of macromolecules from sedimentation and viscosity measurements. Biochim Biophys Acta. 1965 Jul 22;102(2):549–558. doi: 10.1016/0926-6585(65)90145-7. [DOI] [PubMed] [Google Scholar]
  4. DeLange R. J., Fambrough D. M., Smith E. L., Bonner J. Calf and pea histone IV. II. The complete amino acid sequence of calf thymus histone IV; presence of epsilon-N-acetyllysine. J Biol Chem. 1969 Jan 25;244(2):319–334. [PubMed] [Google Scholar]
  5. Ewars P. A., Sooter K. V. Ultracentrifuge tudies of histone fractions from calf thymus deoxyribonucleoprotein. Biochem J. 1969 Sep;114(2):227–235. doi: 10.1042/bj1140227. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Haydon A. J., Peacocke A. R. Sedimentation equilibrium and other physicochemical studies on the lysine-rich fraction of calf thymus histones. Biochem J. 1968 Nov;110(2):243–250. doi: 10.1042/bj1100243. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hnilica L. S., Kappler H. A., Jordan J. J. Assymetry in the distribution of basic amino acid residues in the moderately lysine-rich histone F2b from calf thymus. Experientia. 1970 Apr 15;26(4):353–355. doi: 10.1007/BF01896882. [DOI] [PubMed] [Google Scholar]
  8. Johns E. W. Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem J. 1964 Jul;92(1):55–59. doi: 10.1042/bj0920055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. MARGOLIASH E., LUSTGARTEN J. Interconversion of horse heart cytochrome C monomer and polymers. J Biol Chem. 1962 Nov;237:3397–3405. [PubMed] [Google Scholar]
  10. Ogawa Y., Quagliarotti G., Jordan J., Taylor C. W., Starbuck W. C., Busch H. 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. J Biol Chem. 1969 Aug 25;244(16):4387–4392. [PubMed] [Google Scholar]
  11. PHILLIPS D. M., JOHNS E. W. A FRACTIONATION OF THE HISTONES OF GROUP F2A FROM CALF THYMUS. Biochem J. 1965 Jan;94:127–130. doi: 10.1042/bj0940127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pardon J. F., Wilkins M. H., Richards B. M. Super-helical model for nucleohistone. Nature. 1967 Jul 29;215(5100):508–509. doi: 10.1038/215508a0. [DOI] [PubMed] [Google Scholar]
  13. SCHWERT G. W. The molecular size and shape of the pancreatic proteases. II. Chymotrypsinogen. J Biol Chem. 1951 Jun;190(2):799–806. [PubMed] [Google Scholar]
  14. SQUIRE P. G. A RELATIONSHIP BETWEEN THE MOLECULAR WEIGHTS OF MACROMOLECULES AND THEIR ELUTION VOLUMES BASED ON A MODEL FOR SEPHADEX GEL FILTRATION. Arch Biochem Biophys. 1964 Sep;107:471–478. doi: 10.1016/0003-9861(64)90303-0. [DOI] [PubMed] [Google Scholar]
  15. Teller D. C., Kinkade J. M., Jr, Cole R. D. The molecular weight of lysine-rich histone. Biochem Biophys Res Commun. 1965 Sep 22;20(6):739–744. doi: 10.1016/0006-291x(65)90079-3. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES