Purification and Properties of Dye-linked Aldehyde Dehydrogenase in Rhodopseudomonas acidophila M402(Biological Chemistry)
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概要
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Rhodopseudomonas acidophila M402 grown under aerobic-dark condition shows two bands of dye-linked aldehyde dehydrogenase activity by polyacrylamide gel electrophoresis. The slower-migrating band coincided with the dye-linked aromatic alcohol dehydrogenase that was active on aromatic and aliphatic alcohols and aldehydes. The faster-migrating band was a new dye-linked aldehyde dehydrogenase. The latter enzyme was purified 125-fold by ultracentrifugation and column chromatographies on DEAE-cellulose, Bio-Gel HTP, and Sepharose CL-6B. The enzyme has a relative molecular mass of 70,000 daltons, and a subunit size of 35,000 dalton indicates the dehydrogenase has a dimeric structure. The isoelectric point was pH 4.74. NAD^+ and NADP^+ do not act as electron acceptors. The enzyme was active specifically on straight chain aldehydes (C3-C10) rather than on benzaldehyde and its substitutes. Aromatic and aliphatic alcohols were inert for this enzyme. The Michaelis constant (mM) were 1.6, 0.6, 0.9, 3.6, 0.5, 0.3, 0.1, 0.9, 0.6, 0.3, and 0.1 for benzaldehyde, m-hydroxybenzaldehyde, m-anisaldehyde, vanillin, propionaldehyde, butyraldehyde, hexaldehyde, heptaldehyde, octaldehyde, nonaldehyde, and decaldehyde, respectively.
- 社団法人日本農芸化学会の論文
- 1991-04-23
著者
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Oikawa Tadao
Institute Of Applied Biochemistry The University Of Tsukuba:(present Office)institute For Chemical R
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YAMANAKA Kei
Institute of Applied Biochemistry, The University of Tsukuba
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IINO Hideaki
Institute of Applied Biochemistry, The University of Tsukuba
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Iino Hideaki
Institute Of Applied Biochemistry The University Of Tsukuba
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Yamanaka Kei
Institute Of Applied Biochemistry The University Of Tsukuba:(present Office)department Of Applied Ch
関連論文
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