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DNase II in spermatozoa of the loach misgurnus fossilis L

A deoxyribonuclease (DNase) which is active at acid pH in the absence of bivalent cations was found in loach spermatozoa. The enzyme was purified by ion-exchange chromatography and partially characterized. The DNase has optimal activity at pH 5.5 and its molecular weight is about 30 kD; its substrate is covalently closed circular duplex DNA, and its product is the corresponding unit-length linear DNA. The DNase is inhibited by MgCl2 and activated by EDTA. Thus, this endoDNase found in loach spermatozoa can be classified as a DNase II. The biological role of this DNase II is discussed.