Partial purification and characterization of dipeptidyl-aminopeptidase III fromDictyostelium discoideum |
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| Affiliation: | 1. Division of Nephrology, University of Washington, Seattle, Washington, USA;2. Department of Molecular and Cellular Biology, Roswell Park Cancer Institute, Buffalo, New York, USA;3. Division of Nephrology, Washington University School of Medicine, St. Louis, Missouri, USA;1. Division of Nephrology, Department of Medicine, Duke University School of Medicine, Durham, North Carolina, USA;2. Renal Section, Durham Veterans Affairs Health Care System, Durham, North Carolina, USA;1. Shandong Provincial Qianfoshan Hospital, Shandong University, Jinan, Shandong, China;2. G.W. Hooper Research Foundation, University of California at San Francisco, San Francisco, California, USA |
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| Abstract: | Dipeptidyl-aminopeptidase III was isolated from cells of the cellular slime moldDictyostelium discoideum in the culmination stage of development. The enzyme was purified 18-fold by precipitation with ammonium sulfate and gel filtration chromatography and was shown to have a molecular weight of 158,000 and a sharp pH optimum at pH 10.2 and to be inhibited by sulfhydryl reagents. The enzyme acted upon the artificial substratearginyl-arginyl-β-naphthylamide, producing arginyl-arginine andβ-naphthylamine but notarginyl-β-naphthylamide. Activity towardarginyl-arginyl-β-naphthylamide was strongly inhibited by physiological concentrations of angiotensin III and, to a lesser extent, by angiotensins I and II and other angiotensin-related peptides but not by enkephalin peptides. Several dipeptides known to inhibit mammalian dipeptidyl-aminopeptidase III also inhibited theDictyostelium enzyme. Incubation of the enzyme preparation with angiotensins resulted in their conversion into a complex mixture of products. Thus dipeptidyl-aminopeptidase III fromDictyostelium closely resembles the mammalian enzyme in many of its characteristics. |
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