Abstract
Deoxyribonuclease was isolated from cow snout epidermis and purified approximately 200-fold in specific activity. The enzyme has a pH optimum of 5.5 and a temperature optimum at 50° C. No physiologic cations were required for enzyme activity. Activity was strongly inhibited by zinc sulfate and ammonium sulfate. It was found that the enzyme hydrolyzed native DNA more efficiently than heat denatured DNA. Because the average chain length of the limit digest was approximately 3, the isolated DNase was considered to be an endonuclease acting at many places along the length of the DNA polymer chain. The physiologic role of DNase in nuclear decomposition during epidermal keratinization is discussed.
Published Version
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