计算溶液所需的质量、体积或浓度。
有货
Accession #
P0CS93
为什么选择此级别
EnzymoPure™ 级 ，适用于对基线干扰要求严格的色谱和分析工作流程。
储存与运输
-20°C储存。超低温运输 。请查阅批次 COA 获取详细规格。
质量文档
SDS、COA、产品数据表及规格说明书均可下载。可通过批号查询获取批次 COA。
文献证明
在色谱分析、有机合成和交叉偶联反应领域已被 5 篇同行评审文献引用。
概述
半乳糖氧化酶可作为一种分析工具，用于特异性测定血浆、植物提取物和磷脂中的 D-半乳糖。它可用于表征几种聚合物中的末端 D-半乳糖苷单元。它也可用于测定乳糖含量。
来自树状指孢霉的半乳糖氧化酶已用作阿拉伯半乳聚糖的半乳糖氧化酶处理的组分。它也已用于与过氧化物酶共固定化，以制备用于半乳糖检测的生物传感器。
Galactose oxidase oxidizes galactose and some galactose derivatives in both free and polymeric forms. Oxidation occurs at the C6 position. The enzyme has a molecular weight of 68 ± 3 kDa, and the optimum pH is 7.0.
Useful in the determination of lactose.
Application
Galactose Oxidase from Dactylium dendroides has been used as a component for galactose oxidase treatment of arabinogalactan. It has also been used to co-immobilise with peroxidase for the preparation of a biosensor for galactose detection. Galactose oxidase may be used as an analytical tool for the specific determination of D-galactose in blood plasma, plant extracts, and phospholipids. It could be used for the characterization of terminal D-galactoside units in several polymers. It may also be useful in the determination of lactose.
1、Specificity ：GAO has a wide substrate specificity, but remarkable stereospecificity, only oxidizing D-isomers of substrates (McPherson et al. 1992). GAO will oxidize galactose and some galactose derivatives in both free and polymeric form. Oxidation occurs at the C6 position.
2、Composition：GAO contains one Cu(II) atom yet catalyzes a two-electron transfer reaction (McPherson et al. 1992). The copper is bound by two tyrosines, and two histidines (Tyr272, Tyr495, His496, and His581). In a novel post-translational covalent modification, Tyr272 is linked by a thioether bond to cysteine (Cys228), suggesting the involvement of a tyrosine radical in the catalytic mechanism. Stabilization of the radical occurs because Tyr272 of the thioether bond is liganded to the copper, creating a stacking interaction with Trp290 (Whittaker et al. 1989, Ito et al. 1991, and Whittaker et al. 2005). The structure of the enzyme has revealed extensive beta-sheet secondary structure, consistent with the high stability of the enzyme (Kosman et al. 1974).
Most extracellular proteins of eukaryotes are modified by glycosylation during passage through the ER and golgi, leading to greater glycosylation of extracellular than intracellular forms of a protein. Unusually, the intracellular form of GAO is more highly glycosylated (9% carbohydrate) and exhibits greater stability than the extracellular form (2% carbohydrate) (Medonca and Zancan 1988). Additionally, most proteins are modified by O- and/or N-glycosylation while GAO is only modified only by O-glycosylation (Kornfield and Kornfield 1985, and McPherson et al. 1992)
3、Molecular Characteristics：The gaoA gene contains a long open reading frame from +324 to +2507, including the mature protein-coding sequence (+521 to +2507). It also contains a long untranslated upstream region and a putative pro-sequence with a monobasic cleavage site (McPherson et al. 1992).
4、Characteristics of Galactose Oxidase：
Protein Accession Number：P0CS93；
Isoelectric point：7.75 (Theoretical)
CATH Classification：Three domains:
Class: Mainly Beta
Architecture: Sandwich, 7 Propellor
Topology: Jelly Rolls, Methylamind Dehydrogenase; Chain H, Immunoglobulin-like
Molecular Weight
68.5 kDa (calculated from translated DNA sequence and SDS-polyacrylamide gel electrophoresis, McPherson et al. 1992)
68.0 ± 3.0 kDa (determined from physical measurements, Cooper et al. 1959)
Optimal pH：7.0 (Cooper et al. 1959)
Extinction Coefficient：
122,480 cm-1M-1 (Theoretical)
E1%, 280 = 17.87 (Theoretical)
Inhibitors
Cyanide
Diethyldithiocarbamate
Azide
Hydroxylamine
EDTA
Applications
Quantitative determination of galactose in blood and other biological fluids (Frings and Pardue 1964, Hankin 1966, and Roth et al. 1965)
Locating galactose histochemically (Roberts and Gupta 1965)
Detecting and distinguishing glycoproteins (Itaya et al. 1975)
5、Galactose Oxidase Assay：Method
The reaction velocity is measured in a peroxidase/o-tolidine coupled system as an increase in A425 resulting from the oxidation of galactose. One unit results in a change in A425 of 1.0 per minute at 25°C and pH 6.0 under the defined conditions.
Reagents
0.1 M Potassium phosphate buffer, pH 6.0
0.5% o-tolidine. Note: o-tolidine has been reported to be carcinogenic. Handle with care.
Peroxidase. Dissolve Worthington peroxidase (Code: HPOD) at a concentration of approximately 60 u/ml in reagent grade water.
10% galactose. Allow to come to equilibrium of mutarotation by allowing to stand overnight.
Enzyme
Dissolve at a concentration of 1 mg/ml in reagent grade water. Dilute further for assay to a concentration of 0.2 - 0.5 units/ml.
Procedure
Adjust spectrophotometer to 425 nm and 25°C.
Prepare tolidine-buffer mixture by adding 0.1 ml tolidine to 12 ml 0.1 M potassium phosphate buffer pH 6.0.
Pipette into each cuvette as follows:
Tolidine-buffer solution 1.7 ml
10% Galactose 1.5 ml
Peroxidase 0.1 ml
Incubate in spectrophotometer at 25°C for 3 - 4 mintues to achieve temperature equilibration and establish blank rate, if any. Add 0.1 ml of appropriately diluted enzyme and record increase in A425/min. from initial linear portion of the curve.
规格
产品名称
半乳糖氧化酶 来源于树状指孢霉
别名
半乳糖氧化酶
英文别名
D-Galactose:oxygen 6-oxidoreductase
规格或纯度
EnzymoPure™, ≥30 units/mg dry weight
生化机理
半乳糖氧化酶催化 D-半乳糖转化为 D-半乳糖-己二糖。 2-Deoxy-Dalactose, lactose, melibiose, raffinose and stachyose react with galactose oxidase in the peroxidase:o-tolidine system.基本上没有观察到 D-葡萄糖、L-半乳糖、L-阿拉伯糖或 D-葡萄糖醛酸的氧化作用。
Accession #
CAS编号和信息
9028-79-9
酶学委员会编号
1.1.3.9
分子类型
酶
储存与运输
物理形态
固体
浓度
≥30 units/mg dry weight
储存条件
-20°C储存
运输条件
超低温运输
单位定义
One Unit equals a change in absorbance at 425 nm of 1.000 per minute at 25°C, pH 6.0 using a peroxidase/o-tolidine coupled assay with galactose as the substrate.
技术文档
高级数据
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技术文档和文章
此产品的引用文献
引用文献
| 1. Jiajia Li, Shuang Yue, Ziyuan Gao, Wenhua Hu, Zhaoliang Liu, Guoqiang Xu, Zhen Wu, Xumin Zhang, Guolin Zhang, Fuliang Qian, Junhong Jiang, Shuang Yang. (2023) Novel Approach to Enriching Glycosylated RNAs: Specific Capture of GlycoRNAs via Solid-Phase Chemistry. ANALYTICAL CHEMISTRY, [PMID:37524653] [10.1021/acs.analchem.3c01630] |
| 2. Ziyi Tong, Shengyan Hou, Zhenkun Zhang, Zhen Liu, Yifei Zhang. (2024) Biochemical approaches for decoding the information stored with metabolites. SENSORS AND ACTUATORS B-CHEMICAL, [10.1016/j.snb.2024.136618] |
| 3. Tong Xing, Yaxin Lv, Gongqing Wu, Zhou Zhang, Wanqing Zhang, Xinping Wang, Zhuolang Chen, Weining Zhao, Felipe Conzuelo, Fangyuan Zhao. (2025) A novel biofuel cell based on galactose oxidase and bilirubin oxidase for efficient glycerol conversion and electricity generation. CHEMICAL ENGINEERING JOURNAL, [10.1016/j.cej.2025.163474] |
| 4. Wanqing Zhang, Xiaodong Su, Yaxin Lv, Xuelin Zhao, Zhou Zhang, Yuntong Du, Mengyu Fan, Heshan Zhao, Matthias Rögner, Felipe Conzuelo, Weining Zhao, Mei Li, Fangyuan Zhao. (2026) A Biophotocathode Based on Photosystem I with Record-High Photocurrent Density Coupled with Bioelectrochemical Glycerol Oxidation. ACS Sustainable Chemistry & Engineering, [10.1021/acssuschemeng.5c13204] |
| 5. Hongxu Zhang, Mingyuan Liu, Wenjia Tian, Ke Liu, Mengyao Hao, Hairong Yu, Weikang Sun, Leilei Guo, Xiaoxu Tan, Kaiyu Gao, Tianyi Jiang, Chuanjuan Lü, Qianjin Kang, Cuiqing Ma, Longyang Dian, Ping Xu, Chao Gao. (2026) Enzymatic Synthesis of 3-Hydroxypyruvate and Pyruvate from CO2-Derived C1 Compounds. ACS Catalysis, [10.1021/acscatal.5c08729] |
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