Migration of histones from the nuclei of isolated cerebral tissues kept in cold media

Abstract

Histones were extracted from isolated nuclei of unsliced and sliced cerebral cortex and some of their properties studied. The arginine-rich histone contains at least nine components. The arginine content is 10-11%. Basic proteins from microsomal fractions contain 4-6% arginine. Nuclear histones are lost from nuclear fractions made from sliced cerebral cortex, which has been kept in cold buffered glucose media. Arginine-rich proteins can then be extracted from other subcellular particles of the tissue. Some basic protein also appears in the soluble supernatant proteins. No loss of histones occurred in nuclei from slices not subjected to cold media. Isolated cerebral microsomal fractions bind histones extracted from cerebral cortex nuclei; they also bind calf-thymus histone. It is suggested that the migration of the histone from the nuclei of slices kept in cold media and its combination with acidic microsomal constitutents is involved in the concomitant loss of the tissues''s response to electrical excitation.