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CYTOCHEMICAL DEMONSTRATION OF HISTONASE ACTIVITY IN HUMAN LEUKOCYTES

LAWRENCE KASS 1 and BERTRAM SCHNITZER 2

1 Department of Internal Medicine (Simpson Memorial Institute) The University of Michigan Medical School, Ann Arbor, Michigan 48104
2 Department of Pathology, The University of Michigan Medical School, Ann Arbor, Michigan 48104

A cytochemical technique was devised for demonstrating a lysosomal enzyme capable of hydrolyzing histone. The test for histonase involved incubation of peripheral blood leukocytes in a mixture of calf thymus histone (substrate) and Fe(NH4)2(SO4)2·6H2O. Combination of this iron salt occurred with products of histone cleavage (arginine, lysine, glycine). The iron-amino acid complex was made visible in the cytoplasm of the cell by the Prussian blue stain. Histonase enzyme was found to have a narrow substrate specificity and to react only with histone and not with a variety of biologic and synthetic substrates for protease activity. The role of histonase in the transfer of information from nucleus to cytoplasm is discussed.

Submitted on June 12, 1973


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