Chromatin superstructure. A study with an immobilized trypsin

S. I. Dimitrov, T. M. Apostolova, V. L. Makarov, I. G. Pashev

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Hen erythrocyte chromatin was treated with trypsin immobilized on collagen membranes and the unfolding of chromatin fiber was followed by light scattering at 90° and flow linear dichroism. Chromatin was found almost completely decondensed when the bulk of H1 and H5 was digested while H3 was still intact. Further digestion leading to degradation of both H3 and the rest of H1 and H5 accounted for no more than 10-15% of the total effect. When chromatin with trypsin-cleaved H1 and H5 was titrated with increasing amounts of spermidine it folded similarly to the control sample. This finding suggests that charge neutralization appears a likely mechanism for maintaining the structure of the 30 nm chromatin fiber by the C-terminal domain of H1 and H5.

Original languageEnglish
Pages (from-to)322-326
Number of pages5
JournalFEBS Letters
Volume200
Issue number2
DOIs
Publication statusPublished - 12 May 1986
Externally publishedYes

Fingerprint

Trypsin
Chromatin
Spermidine
Fibers
Light scattering
Digestion
Collagen
Erythrocytes
Membranes
Light
Degradation

Keywords

  • Chromatin structure
  • Flow linear dichroism
  • Immobilized enzyme
  • Light scattering
  • Trypsin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Chromatin superstructure. A study with an immobilized trypsin. / Dimitrov, S. I.; Apostolova, T. M.; Makarov, V. L.; Pashev, I. G.

In: FEBS Letters, Vol. 200, No. 2, 12.05.1986, p. 322-326.

Research output: Contribution to journalArticle

Dimitrov, S. I. ; Apostolova, T. M. ; Makarov, V. L. ; Pashev, I. G. / Chromatin superstructure. A study with an immobilized trypsin. In: FEBS Letters. 1986 ; Vol. 200, No. 2. pp. 322-326.
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