Results 181 to 190 of about 4,782 (205)

Mechanism of the reaction catalyzed by dehydroascorbate reductase from spinach chloroplasts

European Journal of Biochemistry, 2003
Dehydroascorbate 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, Chikahiro, Miyake, Akiho, Yokota   +2 more
openaire   +2 more sources

Molecular Characterization of a Dehydroascorbate Reductase from Pinus bungeana

Journal of Integrative Plant Biology, 2009
Abstract 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, Ying-Ru, Zhao, Cai-Ling, Wang, Zhi-Ling, Yang, Qing-Yin, Zeng, Hai, Lu   +5 more
openaire   +2 more sources

Purification and properties of dehydroascorbic acid reductase of peas (Pisum sativum)

Archives of Biochemistry and Biophysics, 1952
Abstract 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
openaire   +2 more sources

Overexpression of dehydroascorbate reductase, but not monodehydroascorbate reductase, confers tolerance to aluminum stress in transgenic tobacco

Planta, 2009
Aluminum (Al) inhibits plant growth partly by causing oxidative damage that is promoted by reactive oxygen species and can be prevented by improving antioxidant capacity. Ascorbic acid (AsA), the most abundant antioxidant in plants, is regenerated by the action of monodehydroascorbate reductase (MDAR) and dehydroascorbate reductase (DHAR).
Lina, Yin, Shiwen, Wang, Amin Elsadig, Eltayeb, Md Imtiaz, Uddin, Yoko, Yamamoto, Wataru, Tsuji, Yuichi, Takeuchi, Kiyoshi, Tanaka   +7 more
openaire   +2 more sources

Factors Severely Affecting the Dehydroascorbate Reductase Assay

1998
In 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
openaire   +1 more source

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, 1995
The 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
openaire   +1 more source

NADH-dependent dehydroascorbate reductase in the rabbit lens.

The Tokai journal of experimental and clinical medicine, 2002
The 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, M, Bando, H, Obazawa, M, Oka, M, Takehana, S, Kobayashi   +5 more
openaire   +1 more source

Purification and Characterization of a Glutathione Dependent Dehydroascorbate Reductase from Human Erythrocytes

Biochemical and Biophysical Research Communications, 1996
A GSH-dependent dehydroascorbate reductase (EC 1.8.5.1) was purified to homogeneity from human erythrocytes. The enzyme was a monomer of 32 kDa and was purified 133-fold from a crude DEAE-Sepharose fraction with a 25% yield. The reduced protein had a pI of 5.1 as judged by isoelectric focusing. Kinetic analysis gave a Kcat of 316 min-1, a Km of 0.21 mM
D P, Xu, M P, Washburn, G P, Sun, W W, Wells   +3 more
openaire   +2 more sources

Dehydroascorbic Acid Reductase

Industrial & Engineering Chemistry, 1937
E. F. Kohman, N. H. Sanborn
openaire   +1 more source

Molecular and Functional Characterization of Monodehydro-ascorbate and Dehydroascorbate Reductases

2017
When ascorbate (AsA) plays a role in cells as an antioxidant or a substrate for some enzymes including ascorbate peroxidase (APX), it is primarily oxidized to the monodehydroascorbate (MDHA) radical and then dehydroascorbate (DHA) is formed via the disproportionation of MDHA.
openaire   +1 more source