Purification of Dehydroascorbate Reductase from Spinach and Its Characterization as a Thiol Enzyme

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概要

• 論文の詳細を見る

• Dehydroascorbate (DHA) reductase (EC 1.8.5.1) was purified from spinach leaves to nearly a homogeneous state, judging from polyacrylamide gel electrophoresis. The enzyme was found to be a monomer with a molecular weight of 23,000 with apparent K_m values for GSH and DHA of 2.5 and 0.07 mM, respectively. Kinetic studies indicated that the reaction proceeds by an ordered or random mechanism involving the formation of a ternary complex. The enzyme was inhibited by thiol reagents and DHA could partly protect the enzyme thiol group. Incubation of the inactivated enzyme with GSH led to slight recovery of the activity. NADH, NADPH, cysteine or reduced thioredoxin could not replace GSH as an electron donor. Thus, the thiol group(s) participates in the reaction of DHA reductase.

• 日本植物生理学会の論文

著者

• Asada Kozi

  The Research Institute for Food Science, Kyoto University

• Hossain M.

  The Research Institute For Food Science Kyoto University

• Asada Kozi

  The Research Institulefor Fbod Science Kyoto University

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