Purification and properties of a pepstatin-insensitive carboxyl proteinase from a Gram-negative bacterium |
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Institution: | 1. Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan;2. Department of Fragrance and Cosmetic Science, Kaohsiung Medical University, Kaohsiung 807, Taiwan;3. Department of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan;1. Department of Pharmacy, School of Stomatology, The Fourth Military Medical University, Xi''an, Shaanxi 710032, China;2. Department of Pharmacology, Xi''an Jiaotong University College of Medicine, Xi''an, Shaanxi 710061, China;3. Department of Urologic Sciences, University of British Columbia, Vancouver, BC V6H 3Z6, Canada |
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Abstract: | A carboxyl proteinase was found in the culture filtrate of a Gram-negative bacterium. The optimum for the action of the purified enzyme was approx. pH 3 and its caseinolytic activity was not inhibited by carboxyl proteinase inhibitors, such as pepstatin, Streptomyces pepsin inhibitor and diazoacetyl-DL-norleucine methyl ester. 1,2-epoxy-3-(p-nitrophenoxy)propane modified the enzyme with concomitant loss of its enzyme activity. The enzymatic and physicochemical properties of the enzyme were compared with those of known pepstatin- and diazoacetyl-DL-norleucine methyl ester-insensitive carboxyl proteinases previously reported. To our knowledge, this is the first carboxyl proteinase isolated from bacteria. |
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