Affordable Access

Publisher Website

Circular dichroism spectra of putative transcribed and repressed chromatin

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
52
Issue
1
Identifiers
DOI: 10.1016/0006-291x(73)90974-1
Disciplines
  • Biology

Abstract

Abstract Circular dichroism (CD) spectra have been determined for chromatin fractions obtained by ECTHAM-cellulose chromatography. The molecular ellipticity at the positive long wavelength maximum is about 3000 deg cm 2/dmol for early-eluted chromatin fractions, thought to be relatively repressed in vivo , and 5000–6000 deg cm 2/dmol for late-eluted chromatin fractions, those thought to be preferentially transcribable in vivo . CD bands in the peptide bond spectral region also differ for the two chromatin fractions, early-eluted chromatin having a more helical conformation for proteins. In addition to previously known differences in protein content, the biological activity of a native chromatin fraction can now be correlated with the conformation of its DNA.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Circular dichroism spectra of putative transcribed...

on Biochemical and Biophysical Re... May 01, 1973

Circular dichroism spectra and ethidium bromide bi...

on Biochemical and Biophysical Re... Jan 01, 1975

Role of nonhistone chromosomal proteins in determi...

on Archives of Biochemistry and B... August 1975
More articles like this..