Abstract
Affinity chromatography of the calf thymus cysteine-containing histone, rich in arginine and alanine, has been examined basing on the reaction between the SH group and ρ-chloromercuriben-zoated Sepharose. Histories were passed through the column in 5M urea-0.1M citrate buffer, pH 5.5, and the retained fraction was eluted with the denaturant-buffer solution containing 0.05M 2-mercaptoethanol. Further purification of the retained fraction was achieved by Bio-Gel P-60 gel chromatography. The purified fraction showed a single band on polyacrylamide gel electrophoresis and an amino acid in accordance with that obtained by sequence determination.
