Purification and characterization of grass carp mitochondrial aldehyde dehydrogenase |
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| Institution: | 1. Research Center for Tropical and Infectious Diseases, Kerman University of Medical Sciences, Kerman, Iran;2. Department of Medical Mycology and Parasitology, School of Medicine, Medical University of Kerman, Kerman, Iran;3. Department of Parasitology and Mycology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran;4. Basic Sciences in Infectious Diseases Research Center, Department of Parasitology and Mycology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran;1. Laboratório de Estudos Avançados de Microrganismos Emergentes e Resistentes, Departamento de Microbiologia Geral, Instituto de Microbiologia Paulo de Góes, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil;2. Programa de Pós-Graduação em Bioquímica, Instituto de Química, UFRJ, Rio de Janeiro, Brazil;1. Department of Medicine, University of Washington, 1959 NE Pacific St, Seattle, WA 98195, USA;2. Veterans Affairs Puget Sound Health Care System, 1660 S Columbian Way, Seattle, WA 98108, USA;3. Eli Lilly and Company, 893 Delaware St, Indianapolis, IN 46225, USA;4. Department of Anthropology, University of Washington, 1959 NE Pacific St, Seattle, WA 98195, USA;1. Department of Orthodontics, Barts and the London School of Medicine and Dentistry, Queen Mary University, London, United Kingdom;2. Division of Dentistry, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, United Kingdom;1. Bioscience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan;2. Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan;3. Program for Leading Graduate Schools, Integrative Graduate Education and Research Program in Green Natural Sciences, Nagoya University, Nagoya, 464-8601, Japan;4. Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka, 819-0395, Japan |
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| Abstract: | The molecular biology and enzymology of aldehyde dehydrogenase (ALDH) have been extensively investigated. However, most of the studies have been confined to the mammalian forms, while the sub-mammalian vertebrate ALDHs are relatively unexplored. In the present investigation, an ALDH was purified from the hepatopancreas of grass carp (Ctenopharygodon idellus) by affinity chromatographies on α-cyanocinnamate-Sepharose and Affi-gel Blue agarose. The 800-fold purified enzyme had a specific activity of 4.46 U/mg toward the oxidation of acetaldehyde at pH 9.5. It had a subunit molecular weight of 55 000. Isoelectric focusing showed a single band with a pI of 5.3. N-terminal amino acid sequencing of 30 residues revealed a positional identity of ～70% with mammalian mitochondrial ALDH2. The kinetic properties of grass carp ALDH resembled those of mammalian ALDH2. The optimal pH for the oxidation of acetaldehyde was 9.5. The Km values for acetaldehyde were 0.36 and 0.31 μM at pH 7.5 and 9.5, respectively. Grass carp ALDH also possessed esterase activity which could be activated in the presence of NAD+. |
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