Catalase from Aspergillus niger
(Synonyms: 过氧化氢酶) 目录号 : GC60674
Catalase是重要的抗氧化酶,在清除ROS。在维持氧化还原状态的平衡方面发挥着重要作用。Catalase与肿瘤的发生,发展关系密切。有潜力用于肿瘤的预防研究。
Cas No.:9001-05-2
Sample solution is provided at 25 µL, 10mM.
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Catalase is a key enzyme in the metabolism of H2O2 and reactive oxygen species (ROS), and its expression and localization is markedly altered in tumors[1]. Free oxygen radical scavenger.
Catalase, the enzyme that metabolizes H2O2 but also reacts with a multitude of other substrates. The active site of catalase contains an iron atom. Human catalase contains four identical subunits, each subunit containing four distinct domains and one prosthetic heme group. The four domains include: (1) a N-terminal arm which contains a distal histidine, an essential amino acid for the catalase reaction; (2) a β-barrel domain that contains eight β-barrels arranged in an antiparallel fashion with six α-helical insertions, conferring the hydrophobic core of the protein necessary for the tri-dimensional structure of the enzyme; (3) a connection domain which contains the tyrosine residue that binds the heme group; and finally (4) an α-helical domains, which is important for NADPH binding[1].
References:
[1]. Glorieux C, et al. Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach. Biol Chem. 2017 Sep 26;398(10):1095-1108.
| Cas No. | 9001-05-2 | SDF | |
| 别名 | 过氧化氢酶 | ||
| Canonical SMILES | [Catalase] | ||
| 分子式 | 分子量 | ||
| 溶解度 | Water: 33.33 mg/mL ; DMSO: < 1 mg/mL (insoluble or slightly soluble) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Properties of Aspergillus niger catalase
J Biochem 1982 Nov;92(5):1449-56.PMID:7153210DOI:10.1093/oxfordjournals.jbchem.a134069.
Catalase from Aspergillus niger was purified to homogeneity as judged from the results of ultracentrifugation and polyacrylamide gel electrophoresis. The enzyme had a molecular weight of 385,000 as estimated from sedimentation measurements. Carbohydrate analyses showed that the catalase was a glycoprotein containing about 8.3% neutral sugar and 1.9% glucosamine. Under denaturing conditions, polyacrylamide gel electrophoresis revealed only one band with a molecular weight of 97,000 daltons in gels stained for either protein or sugar, suggesting that the native enzyme consists of four subunits with covalently bound carbohydrate. In the reaction with inhibitors, A. niger catalase showed lower affinity than the "standard" catalases. The pK values for HCN, HN3, and HF were estimated to be 3.4 (at pH 7.4), 2.3, and 1.5 (at pH 4.2), respectively. In addition, the fungal enzyme reacts with methyl hydrogen peroxide in a very unusual way. Even after the addition of a large excess of the peroxide, only catalase compound I was formed, and compound II did not appear. Using this unique property of A. niger catalase, we obtained CD and MCD spectra of compound I uncontaminated by compound II. The magnitude of the positive CD peak of compound I in the Soret region was about half that of the native enzyme. The MCD spectrum obtained was better resolved than that of bovine liver catalase compound I in the visible region.
The catR gene encoding a Catalase from Aspergillus niger: primary structure and elevated expression through increased gene copy number and use of a strong promoter
Mol Microbiol 1993 Sep;9(5):989-98.PMID:7934925DOI:10.1111/j.1365-2958.1993.tb01228.x.
Synthetic oligonucleotide probes based on amino acid sequence data were used to identify and clone cDNA sequences encoding a catalase (catalase-R) of Aspergillus niger. One cDNA clone was subsequently used to isolate the corresponding genomic DNA sequences (designated catR). Nucleotide sequence analysis of both genomic and cDNA clones suggested that the catR coding region consists of five exons interrupted by four small introns. The deduced amino acid sequence of catalase-R spans 730 residues which show significant homology to both prokaryotic and eukaryotic catalases, particularly in regions involved in catalytic activity and binding of the haem prosthetic group. Increased expression of the catR gene was obtained by transformation of an A. niger host strain with an integrative vector carrying the cloned genomic DNA segment. Several of these transformants produced three- to fivefold higher levels of catalase than the untransformed parent strain. Hybridization analyses indicated that these strains contained multiple copies of catR integrated into the genome. A second expression vector was constructed in which the catR coding region was functionally joined to the promoter and terminator elements of the A. niger glucoamylase (glaA) gene. A. niger transformants containing this vector produced from three- to 10-fold higher levels of catalase-R than the untransformed parent strain.
Purification of extracellular Catalase from Aspergillus niger
Acta Microbiol Pol 1998;47(1):31-43.PMID:9691429doi
The extracellular catalase (EC 1.11.1.6) produced by Aspergillus niger culture in 5-liter fermentor was isolated and purified by ion-exchange chromatography on DEAE Sepharose (fast flow) column, hydrophobic interaction on phenyl-Sepharose column and chromatofocusing on PBE 94 column. Some physico-chemical properties of two purified catalase forms were also determined (molecular weight, isolelectric point, polysaccharides contents, Km, and Ea).
The activation of Aspergillus niger catalase by sodium n-dodecyl-sulphate
Biochim Biophys Acta 1987 Jul 7;913(3):395-8.PMID:3593744DOI:10.1016/0167-4838(87)90151-8.
In marked contrast to most enzymes it is found that at pH 6.4 the activity of the fungal Catalase from Aspergillus niger is increased on binding of sodium n-dodecyl sulphate (SDS). Activation of the enzyme by up to 180% is found under optimum conditions when approx. 150 SDS molecules are bound. Activation does not occur under acid (pH 3.2) or alkaline (pH 10.0) conditions. Sedimentation analysis confirms that the enzyme does not dissociate into subunits at pH 6.4 (or pH 10.0). These observations are considered in the light of other catalase-SDS studies and it is suggested that the binding of SDS to Aspergillus niger catalase at pH 6.4 results in a small conformational change facilitating the enzymic reaction.