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Catalase from bovine liver(2000-5000u/mg) Sale

(Synonyms: 过氧化氢酶) 目录号 : GC64933

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。

Catalase from bovine liver(2000-5000u/mg) Chemical Structure

Cas No.:9001-05-2

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1g
¥450.00
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产品描述

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.

Chemical Properties

Cas No. 9001-05-2 SDF
别名 过氧化氢酶
Canonical SMILES [Catalase]
分子式 分子量
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Research Update

Interaction between pyridine adenine dinucleotides and bovine liver catalase: a chromatographic and spectral study

Arch Biochem Biophys 1986 Jul;248(1):71-9.PMID:3015030DOI:10.1016/0003-9861(86)90402-9.

Two different fractions were present in crystalline bovine liver catalase, and could be resolved using dye-ligand affinity chromatography with Red-A Matrex gel containing Procion HE 3B. The major part (alpha) was not adsorbed on this gel. The second fraction (beta) was firmly adsorbed to the gel, and could be eluted either by high salt or by NADPH in the micromolar range. Elution of catalase beta was also obtained with NADH, NADP+, and ADP at higher concentration. Fractions alpha and beta displayed no detectable difference in specific activity, stability to heat, and light absorption data. It is suggested that the difference in behavior between alpha and beta is related to the binding of NADPH to the mammalian catalase [H. N. Kirkman and G. F. Gaetani (1984) Proc. Natl. Acad. Sci. USA 81, 4343-4347], and that the beta fraction corresponds to the enzyme molecules that have at least one free site for NADPH binding. Modifications of catalase molecules in the presence of dithioerythritol (DTE) were examined using light absorption and EPR data. Thiol induced changes that corresponded to the formation of catalase complex II. They were partially reversed by NADPH at very low level, and the dinucleotide appeared to be oxidized in this process. DTE-treated bovine catalase was totally adsorbed on the Red-A Matrex columns, and could be eluted as fraction beta. Similar spectral changes in the presence of DTE and NADPH were displayed by a bacterial catalase from Proteus mirabilis. This enzyme was also able to oxidize NADPH, but was not adsorbed by Red-A Matrex. This work suggests that dye-affinity chromatography provides a very convenient tool for isolating dinucleotide-depleted Catalase from bovine liver, facilitating further study of the physiological function of this cofactor within the enzyme.