Resynthesis of Histone Peptide Bonds on a DNA Matrix

  • I. O. Walker
  • S. G. Davies
  • P. N. Schofield
Part of the NATO ASI Series book series (NSSA, volume 101)

Abstract

Digestion of core chromatin with trypsin leads to degradation of the basic amino and carboxyl terminal ends and the production of five large polypeptide fragments which are protected from further tryptic attack by their interactions with DNA. The small basic oligopeptides produced by the trypsin dissociate from the DNA whereas the large, protected fragments remain bound (1). Subsequent digestion of these bound, trypsin resistant polypeptides with chymotrypsin produces further degradation to smaller peptides which still remain bound to the DNA. Double digestion of core chromatin with trypsin and chymotrypsin does not cause any change in the secondary structure of the bound peptides, as monitored by ellipticity at 220 nm (reference 1, and unpublished data of I.O. Walker).

Keywords

Hydrolysis Amide Fluoride Carboxyl Phenyl 

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References

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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • I. O. Walker
    • 1
  • S. G. Davies
    • 2
  • P. N. Schofield
    • 3
  1. 1.Department of BiochemistryUniversity of OxfordOxfordEngland
  2. 2.Dyson Perrins LaboratoryOxfordEngland
  3. 3.Imperial Cancer Research FundLondonEngland

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