Abstract
Abstract Although deoxyribonuclease II (acid DNase) is a widely distributed lysosomal enzyme, the liver enzyme has not been highly purified or well characterized. A procedure is presented for purifying the rat liver lysosomal enzyme 43,000-fold, employing chromatographic fractionations of an extract made from lysosomes. The purified enzyme is free of all other lysosomal enzymes assayed, including phosphatases, other nucleases, and, especially, phosphodiesterase, which has frequently been reported in DNase preparations.
Highlights
Because so many highly purified or well characterized
Deoxvribonuclease II is a lysosomal enzyme [1, 2] f;eq,uently used as a marker enzyme in the subcellular fractionation of cellular homogenates, and its participation in the lysosomal degradation of DNA seems evident from recent studies [3]
The hog spleen enzyme has been stated to be homogeneous [4] ; it is not possible for us to calculate the fold purification of this preparation above the tissue level
Summary
Sirable to purify and characterize the DNase of liver lysosomes. Deoxyribonuclease II (acid DNase) is a widely distributed lysosomalenzyme, the liver enzyme has not been. The rat liver enzyme was chosen for isolation relevant studies are done with this species. Because so many highly purified or well characterized. A procedure is presented for purifying the rat liver lysosomal enzyme 43,000-
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