Purification and Characterization of Cystine Lyase a from Broccoli Inflorescence
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概要
- 論文の詳細を見る
One of the three isoforms of an enzyme degrading L-cystine was purified to homogeneity from broccoli (Brassica oleracea var. italica) inflorescences, with use of a sensitive assay based on derivatization of a reaction product with monobromobimane. The reaction product with a thiol group was found to be thiocysteine from results of liquid chromatography-mass spectrometry and high-resolution mass spectrometry. Pyruvate was also a reaction product, formed in equimolar amounts. The purified enzyme catalyzed β-elimination of L-cystine to yield thiocysteine, pyruvate and possibly ammonia, so it was cystine lyase a. L-Cystine but not D-cystine was a substrate of the enzyme. S-Methyl L-cysteine sulfoxide and S-ethyl L-cysteine sulfoxide were substrates but were less suitable than L-cystine. L- and D-cysteine and also cystathionine were not substrates. The purified enzyme (M 186,000) was composed of four identical subunits (M_r 45,000) and was pyridoxal 5'-phosphate-dependent.
- 社団法人日本農芸化学会の論文
- 1997-11-23
著者
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Ukai Kazuyo
Tohoku Pharmaceutical University
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UKAI Koji
Division of Gastroenterology, Department of Internal Medicine, Nagoya University Graduate School of
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Ukai K
Tokyo Univ. Fisheries Tokyo Jpn
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Ukai Koji
Division Of Gastroenterology Department Of Internal Medicine Nagoya University Graduate School Of Me
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Sekiya Jiro
Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University
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Sekiya Jiro
Division Of Applied Life Sciences Graduate School Of Agricultural Sciences Kyoto University
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