Purification and Characterization of Ferredoxin-Sulfite Reductase from Turnip (Brassica rapa) Leaves and Comparison of Properties with Ferredoxin-Sulfite Reductase from Turnip Roots
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概要
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Ferredoxin-sulfite reductase (Fd-SiR) [hydrogen-sulfide: ferredoxin oxidoreductase, EC 1.8.7.1] from turnip leaves (SiR-L) has been purified to homogeneity and its enzymatic properties compared with that from turnip roots (SiR-R). Each enzyme had a molecular mass of 64.5±0.5 kDa by SDS-PAGE and an isoelectric point of 5.15±0.05. Although each had a pH optimum around 7.8 with the same effects of inhibitors, SiR-L had higher heat stability at 60℃ than SiR-R. Moreover, SiR-R had a lower K_m and a higher specificity constant (k_<cat>/K_m) for turnip leaf ferredoxin than SiR-L. The N-terminal amino acid sequence of SiR-L was different from that of SiR-R. The results of amino acid analysis and peptide mapping suggested that SiR-L and SiR-R have different primary structures.
- 社団法人日本農芸化学会の論文
- 1997-09-23
著者
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TAKAHASHI SHUNJI
Department of Anesthesiology, Nagasaki University School of Medicine
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Takahashi S
Akita Res. Inst. Food And Brewing Akita
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TAMURA Goro
Department of Agricultural Chemistry, Faculty of Horticulture, Chiba University
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Tamura Goro
Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University
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Tamura Goro
Department Of Agricultural Chemistry Faclty Of Horticulture Chiba University
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YIP Wai-Cheung
Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University
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Yip Wai-cheung
Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University
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Takahashi Shunji
Department Of Anesthesiology Nagasaki University School Of Medicine
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Tamura G
Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University
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Suzuki Takahito
Biological Laboratory Faculty Of Science Nara Women's University
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