Purification and Properties of Bile Acid Sulfate Sulfatase from Pseudomonas testosteroni
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概要
- 論文の詳細を見る
The bile acid sulfate sulfatase (BSS) produced by Pseudomonas testosteroni was purified and characterized. Chromatofocusing behavior and amino acid sequence over twelve amino acid residues from N-terminus of the enzyme indicated that BSS was composed of two isoforms of which molecular weights were 125,000 and 103,000. Each isoform was a homodimer of a subunit of which molecular weight was 53,000 or 51,000, respectively. The optimum pH was 8.5 and BSS was stable at pH 5. 8-8.0. The thermostability above 32℃ was improved by the addition of polyols, such as sorbitol, sucrose, and glycerol. BSS was a Mn^<2+>-dependent enzyme and contained 1-2 atoms of manganese in its own protein molecule. All 3α-sulfate esters of the bile acids routinely appearing in human serum were hydrolyzed by BSS to 3β-hydroxyl iso-compounds corresponding to each bile acid and sulfuric acid. We tentatively named this novel enzyme BSS (bile acid 3α-sulfate sulfohydrolase).
- 社団法人日本農芸化学会の論文
- 1994-05-23
著者
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TSUKADA Yoji
Kyoto Research Laboratories, Marukin Shoyu Co., Ltd.
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Matsuda K
Waseda Univ. Tokyo Jpn
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TAZUKE Yasuhiko
Kyoto Research Laboratories, Marukin Shoyu Co., Ltd.
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MATSUDA Kumiko
Kyoto Research Laboratories, Marukin Shoyu Co., Ltd.
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ADACHI Kenichi
Kyoto Research Laboratories, Marukin Shoyu Co., Ltd.
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Tsukada Y
Marukin Bio Inc.
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Tsukada Yoji
Kyoto Research Laboratories Marukin Shoyu Co. Ltd.
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Matsuda K
Department Of Agricultural Chemistry Faculty Of Agriculture Kinki University
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Tazuke Y
Kyoto Research Laboratories Marukin Shoyu Co. Ltd.
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Tazuke Yasuhiko
Kyoto Research Laboratories Marukin Shoyu Co. Ltd.
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