PMID: 2476Feb 2, 1976

Subcellular distribution of histone-degrading enzyme activities from rat liver

European Journal of Biochemistry
P C HeinrichM Jusic


Chromatin prepared from liver tissue contains a histone-degrading enzyme activity with a pH optimum of 7.5-8.0, whereas chromatin isolated from purified nuclei is devoid of it. The histone-degrading enzyme activity was assayed with radioactively labelled total histones from Ehrlich ascites tumor cells. Among the different subcellular fractions assayed, only lysosomes and mitochondria exhibited histone-degrading enzymes. A pH optimum around 4.0-5.0 was found for the lysosomal fraction, whereas 7.5-8.0 has been found for mitochondria. Binding studies of frozen and thawed lysosomes or mitochondria to proteinase-free chromatin demonstrate that the proteinase associated with chromatin isolated from frozen tissue originates from damaged mitochondria. The protein degradation patterns obtained after acrylamide gel electrophoresis are similar for the chromatin-associated and the mitochondrial proteinase and different from that obtained after incubation with lysosomes. The chromatin-associated proteinase as well as the mitochondrial proteinase are strongly inhibited by 1.0 mM phenylmethanesulfonyl fluoride. Weak inhibition is found for lysosomal proteinases at pH 5. Kallikrein-trypsin inhibitor, however, inhibits lysosomal proteinase act...Continue Reading


Feb 10, 1975·Biochimica Et Biophysica Acta·O H DestreeR Charles
Aug 27, 1968·Biochimica Et Biophysica Acta·M FurlanA Suhar
Jan 1, 1974·Methods in Enzymology·A Trouet
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Aug 1, 1956·The Biochemical Journal·C DE DUVE, R WATTIAUX


Mar 1, 1978·The Journal of Cell Biology·T E MillerA O Pogo
Nov 2, 1978·European Journal of Biochemistry·R Haas, P C Heinrich
Nov 1, 1980·Journal of Neurochemistry·T Yanagihara
Dec 1, 1976·Archives of Biochemistry and Biophysics·M JusicP C Heinrich
Jun 16, 1980·Biochemical and Biophysical Research Communications·H HagiwaraT Horio
May 2, 1979·European Journal of Biochemistry·R Haas, P C Heinrich

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