A rat skin acid esteroprotease hydrolyzing benzoylarginine ethylester: purification and properties

A benzoylarginine ethylester hydrolyzing enzyme from rat skin has been purified 54-fold by chromatography on arginine methylester-CH-Sepharose and Sephadex G-200 prior to isoelectrofocusing. The molecular weight of the enzyme is approximately 125,000. The enzyme hydrolyzes bensoylarginine ethylester, acetyltyrosine ethylester, benzoylarginine methylester, benzoyllysine methylester, and benzoylalanine methylester. Casein is slightly hydrolyzed at an optimum pH of 6.5. The enzyme is inhibited by diisopropylfluorophosphate, and p-chloromercuribenzoic acid. KC1 enhances the extraction of the enzyme, increased its activity, and is essential for its stability.