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.
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