Results 191 to 200 of about 7,898 (228)
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Molecular Characterization of a Dehydroascorbate Reductase from Pinus bungeana
Journal of Integrative Plant Biology, 2009Abstract Dehydroascorbate reductase (DHAR) plays a critical role in the ascorbate‐glutathione recycling reaction for most higher plants. To date, studies on DHAR in higher plants have focused largely on Arabidopsis and agricultural plants, and there is virtually no information on the molecular characteristics of DHAR in gymnosperms.
Hai-Ling, Yang +5 more
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Factors Severely Affecting the Dehydroascorbate Reductase Assay
1998In plant cells the photosynthetic electron transport system is the major source of active oxygen. To avoid oxygen mediated toxicity, chloroplasts possess a high activity of active oxygen scavenging system called the ascorbate-glutathione cycle (AGC).
Shunichi Takahashi, Hideo Yamasaki
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Purification and properties of dehydroascorbate reductase from spinach leaves
Phytochemistry, 1977Abstract Dehydroascorbate reductase was detected in the leaves of several plants and has been partially purified from spinach leaves. The enzyme has a MW of ca 25 000, a pH optimum of 7.5, a Km for glutathione (GSH) of 4.43 ± 0.4 mM and a Km for dehydroascorbate of 0.34 ± 0.05 mM. High concentrations of dehydroascorbate inhibit the enzyme.
Christine H. Foyer, Barry Halliwell
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Dehydroascorbate reductase activity in bovine lens.
International journal for vitamin and nutrition research. Internationale Zeitschrift fur Vitamin- und Ernahrungsforschung. Journal international de vitaminologie et de nutrition, 1995The bovine lens was studied for the presence of dehydroascorbate reductase activity. The activity was found to be restricted primarily to the mitochondrial fraction isolated from the cortex-epithelial fraction of the tissue. It was not detectable in the cytosolic fraction. The Km of reaction with dehydroascorbate was approximately 0.45 mM.
C, Rose, P S, Devamanoharan, S D, Varma
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Mechanism of the reaction catalyzed by dehydroascorbate reductase from spinach chloroplasts
European Journal of Biochemistry, 2003Dehydroascorbate reductase (DHAR) reduces dehydroascorbate (DHA) to ascorbate with glutathione (GSH) as the electron donor. We analyzed the reaction mechanism of spinach chloroplast DHAR, which had a much higher reaction specificity for DHA than animal enzymes, using a recombinant enzyme expressed in Escherichia coli.
Taise, Shimaoka +2 more
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Purification and properties of dehydroascorbic acid reductase of peas (Pisum sativum)
Archives of Biochemistry and Biophysics, 1952Abstract Dehydroascorbic acid reductase in pea seeds was purified by fractional precipitation from the pressed pea juice. The preparation was lyophilized and used in the study of some of its properties. The reductase was very unstable at the higher temperatures. At 40 °C. or higher, the enzyme was very rapidly inactivated.
M, YAMAGUCHI, M A, JOSLYN
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Expressional characterization of dehydroascorbate reductase cDNA in transgenic potato plants
Journal of Plant Biology, 2008In plants ascorbic acid (AsA) is a strong antioxidant or reductant that can be converted to dehydroascorbate (DHA) by oxidation. DHA, a very short-lived chemical, can either be hydrolyzed irreversibly to 2,3-diketogulonic acid or recycled to AsA by dehydroascorbate reductase (DHAR).DHAR cDNA, isolated from sesame hairy roots, was inserted into two ...
Young-Min Goo +9 more
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NADH-dependent dehydroascorbate reductase in the rabbit lens.
The Tokai journal of experimental and clinical medicine, 2002The present investigation demonstrates the existence of NADH-dependent dehydroascorbate (DHA) reductase activity in the soluble fraction of the rabbit lens. This DHA reductase was specific for NADH, and its apparent Km values for DHA and NADH were 5.7 mM and 4.0 microM, respectively.
I, Akatsuka +5 more
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Dehydroascorbic Acid Reductase
Industrial & Engineering Chemistry, 1937E. F. Kohman, N. H. Sanborn
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[Molecular characterizations of two dehydroascorbate reductases from Selaginella moellendorffii].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2012Plant dehydroascorbate reductase (DHAR) is a physiologically important reducing enzyme in the ascorbate-glutathione recycling reaction. In this study, two DHARs genes (SmDHAR1 and SmDHAR2) were isolated from Selaginella moellendorffii. The SmDHAR1 and SmDHAR2 genes encode two proteins of 218 and 241 amino acid residues, with a calculated molecular mass
Zishuo, Cheng +4 more
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