Vitamin Related Kit

Dehydroascorbic acid (DHA) is the oxidized form of ascorbic acid (Vitamin C, AsA). AsA serves as an important physiological indicator in plant cells. Changes in AsA content, redox status (AsA/DHA ratio), and the activity of enzymes related to its synthesis and metabolism are involved in plant responses to a range of environmental stresses. DHA is the reversible oxidized form of AsA. Within organisms, DHA and ascorbic acid together constitute a redox system, functioning as an electron acceptor.

Ascorbate oxidase (AAO) is a copper-containing enzyme located in the cytoplasm or bound to the cell wall. Ascorbate oxidase plays an important role in material metabolism within plants. It is not only related to plant growth, development,fruit storage, it is also associated with anti-aging. Catalyzed by ascorbate oxidase, molecular oxygen can oxidize ascorbic acid to dehydroascorbic acid, which can be reduced by cytochrome b on the plasma membrane. The transmembrane transport of electrons in this process can promote cell growth.

Dehydroascorbate reductase (DHAR) is present in the cytoplasm, mitochondria, and chloroplasts. DHAR catalyzes the reduction of dehydroascorbic acid (DHA) by glutathione (GSH) to produce ascorbic acid (AsA) and oxidized glutathione (GSSG), regulating the cellular AsA/DHA ratio. It is a key enzyme in the ascorbate-glutathione redox cycle. Enhancing DHAR activity in plants can increase AsA content in plant-based foods, thereby improving their nutritional quality.

Ascorbate oxidase (AAO) is a copper-containing enzyme located in the cytoplasm or bound to the cell wall. Ascorbate oxidase plays an important role in material metabolism within plants. It is not only related to plant growth, development,fruit storage, it is also associated with anti-aging. Catalyzed by ascorbate oxidase, molecular oxygen can oxidize ascorbic acid to dehydroascorbic acid, which can be reduced by cytochrome b on the plasma membrane. The transmembrane transport of electrons in this process can promote cell growth.

Dehydroascorbate reductase (DHAR) is present in the cytoplasm, mitochondria, and chloroplasts. DHAR catalyzes the reduction of dehydroascorbic acid (DHA) by glutathione (GSH) to produce ascorbic acid (AsA) and oxidized glutathione (GSSG), regulating the cellular AsA/DHA ratio. It is a key enzyme in the ascorbate-glutathione redox cycle. Enhancing DHAR activity in plants can increase AsA content in plant-based foods, thereby improving their nutritional quality.

Dehydroascorbic acid (DHA) is the oxidized form of ascorbic acid (Vitamin C, AsA). AsA serves as an important physiological indicator in plant cells. Changes in AsA content, redox status (AsA/DHA ratio), and the activity of enzymes related to its synthesis and metabolism are involved in plant responses to a range of environmental stresses. DHA is the reversible oxidized form of AsA. Within organisms, DHA and ascorbic acid together constitute a redox system, functioning as an electron acceptor.

Ascorbate Peroxidase (APX) is one of the important antioxidant enzymes for scavenging reactive oxygen species in plants, and also one of the key enzymes in ascorbate metabolism. APX has multiple isozymes, localized in the chloroplast, cytosol, mitochondria, peroxisomes and glyoxysomes, as well as the peroxisomal and thylakoid membranes. APX catalyzes the oxidation of AsA by H₂O₂ and is the main consumer of AsA in plants. The activity of APX directly affects the content of AsA, and there is a certain negative correlation between APX and AsA.

Ascorbate Peroxidase (APX) is one of the important antioxidant enzymes for scavenging reactive oxygen species in plants, and also one of the key enzymes in ascorbate metabolism. APX has multiple isozymes, localized in the chloroplast, cytosol, mitochondria, peroxisomes and glyoxysomes, as well as the peroxisomal and thylakoid membranes. APX catalyzes the oxidation of AsA by H₂O₂ and is the main consumer of AsA in plants. The activity of APX directly affects the content of AsA, and there is a certain negative correlation between APX and AsA.