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- Roche
- 11136364103
- 2025年08月25日
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- 文献和实验
- 技术资料
- 供应商：
嵘崴达
- 保存条件：
见说明书
- 库存：
需确认
- 英文名：
Ascorbate Oxidase GOT-deficient
- 保质期：
见说明书
from Cucurbita species, poor of Aspartate aminotran-
ferase (AST/GOT), lyophilizate
Oxidoreductase that oxidizes ascorbic acid to dehydroascorbate.
Application
Use Ascorbate Oxidase in a variety of diagnostic tests to eliminate the interfer-
ence of ascorbic acid, since ascorbic acid interferes with the Trinder reaction
that is widely used for the colorimetric determination of analytes. It is useful
in liquid as well as dry chemistry test, e.g., for the determination of uric acid,
lactate, creatine kinase or transaminases.
Benefits
Rely on the tested deficiency of aspartate transaminase. ■
Rely on the proven diagnostic quality of this product. ■
EC 1.10.3.3
Properties
Nomenclature: L-ascorbate:oxygen oxidoreductase
Molecular weight: Approximately 140 kD
Isoelectric point: 5.0-6.0
Michaelis constant (Phosphate buffer, pH 5.6, +25°C):
L-ascorbate: 3 x 10 -4 mol/l
Inhibitors: 4-chloromercuribenzoate, CN - , Na 2 S, diethyl-dithiocarbamate,
8-hydroxyquinoline, K-ethylxanthate
pH optimum: 5.6-7.0 (see figure)
Temperature dependence: See figure
pH stability: 6.5-9.0 (see figure)
Thermal stability: Up to +70°C (see figure)
Stability of the lyophilizate: Stable at +35°C for at least 3 weeks (see figure).
Stability in solution: See figure
Specificity: Several analogs of ascorbate react.
Remark: A decrease in activity of approximately 10% may occur.
Specification
Appearance: Turquoise lyophilizate
Solubility: Clear, slightly turquoise solution in water (c=50 mg/ml)
pH value (c=50 mg/ml in water): 7.0-8.0
Activity (+25°C, L-ascorbate): ≥170 U/mg lyophilizate
Specific activity (+25°C): ≥1,700 U/mg protein
Activity (+37°C, L-ascorbate): ≥180 U/mg lyophilizate
Specific activity (+37°C): ≥1,800 U/mg protein
Protein (BCA): 0.08-0.14 mg/mg lyophilizate
Contaminants (+25°C, expressed as percentage of Ascorbate Oxidase
activity):
Catalase: ≤0.2
Aspartate aminotransferase (AST/GOT): ≤0.0003
Alanine aminotransferase (ALT/GPT): ≤0.0005
Contaminating oxidases (FOX): ≤0.0002
Stability: At -15 to -25°C within specification range for 12 months. Store dry.
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文献和实验催化 L-抗坏血酸氧化生成脱氢抗坏血酸反应的好氧性氧化酶。 EC1． 10． 3． 3。不生成过氧化氢。可在高等植物（例如十字花科、黄瓜、南瓜）及肾上腺皮质中找到。纯化标准样品是蓝绿色的蛋白质，分子量约 14万，含有 0.46— 0.52%的 Cu（每个酶分子平均 10— 12个原子）。也作用于 D-阿拉伯糖型抗坏血酸、葡糖型抗坏血酸。据认为它能还原由多酚氧化酶生成的 o-醌，成为植物呼吸系统的一环。
L-抗坏血酸曾作为治疗远航海员易患的坏血病的维生素（抗坏血病维生素）而被发现的，也称维生素 C，已糖醛酸。最大紫外吸收为 265毫微米（水溶液），氧化还原电位 E0′ =0.166V（ pH=4.0， 35℃）。在新鲜的水果（柑桔、柠檬、葡萄）或蔬菜（西红柿、卷心菜）、绿茶中含量均较多，在动物体内肾上腺中特别多，肝脏、脑垂体、黄体、胸腺等含量也很高。通过各种氧化剂、游离氧（在铜的存在条件下）、多酚氧化酶以及专一的抗坏血酸氧化酶等的作用，容易进行
- 抑制。和抗坏血酸氧化酶一起，借助氧使酚类氧化，所产生的苯醌类在醌还原酶的作用下可被谷胱甘肽和 NADPH等还原，构成一种电子传递系统。如果发生象马铃薯块茎切口那样的细胞损伤，由于绿原酸和酪氨酸的氧化产生的醌不能还原，而聚合生成黑素变成褐色。
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