
It has been found that histone octamer of calf thymus (H2A--H2B--H3--H4)2 can exist in two structural states--"loose" (2M NaCl) and "compact" one (4M NaCl). The compact state of the octamer is characterized by screening of part of tyrosyls for quenching effect of ions I-, longer relaxation time of tyrosyls, greater stability of histone H3 towards trypsinolysis, complete absence of interactions between histone H3 SH-groups and parachlormercuribenzoate.
Histones, Kinetics, Spectrometry, Fluorescence, Macromolecular Substances, Hydrolysis, Animals, Cattle, Electrophoresis, Polyacrylamide Gel, Trypsin, Thymus Gland
Histones, Kinetics, Spectrometry, Fluorescence, Macromolecular Substances, Hydrolysis, Animals, Cattle, Electrophoresis, Polyacrylamide Gel, Trypsin, Thymus Gland
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