Purification and properties of methyl sulfoxide reductases from rat kidney |
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| Authors: | H Fukazawa H Tomisawa S Ichihara M Tateishi |
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| Institution: | 1. Department of Cardiovascular Dynamics, National Cerebral and Cardiovascular Center, Osaka 565-8565, Japan;2. Division of Cardiology, Department of Medicine, Faculty of Medicine, Kinki University, Osaka 589-8511, Japan;1. Department of Nanobiomedical Science & BK21 PLUS Global Research Center for Regenerative Medicine, Dankook University, 29 Anseo-Dong, Cheonan 330-714, Republic of Korea;2. Department of Oral Biochemistry, The School of Dentistry, Dankook University, 29 Anseo-Dong, Cheonan 330-714, Republic of Korea;3. Department of Integrative Bioscience and Biotechnology, Sejong University, Seoul 143-747, Republic of Korea;1. Department of Ecophysiology and Aquaculture, Leibniz-Institute of Freshwater Ecology and Inland Fisheries, Berlin, Germany;2. Department of Endocrinology, Institute of Biology, Humboldt-University Berlin, Berlin, Germany |
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| Abstract: | Two kinds of enzymes (tentatively designated methyl sulfoxide reductases I and II) responsible for the reduction of the methyl sulfoxide group on various xenobiotics have been purified about 223- and 155-fold, respectively, from rat kidney cytosol. The molecular weight was determined to be 12,000 +/- 1000 for methyl sulfoxide reductase I and 24,000 +/- 1000 for methyl sulfoxide reductase II. Thioredoxin or dithiothreitol is essential in order for the reducing activity to occur. The respective Km values of p-bromophenylmethyl sulfoxide were 2.75 and 1.30 mM for methyl sulfoxide reductases I and II. Replacement of the methyl group on the sulfur atom with a longer alkyl group or phenyl group caused a markedly low or negligible substrate activity. |
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