基本描述

产品名称	L-氨基酸氧化酶来源于东部菱背响尾蛇毒液
别名	L-氨基酸：氧气氧化还原酶(脱氨)
英文别名	L-AAO \| L-Amino acid：oxygen oxidoreductase(deaminating)
规格或纯度	EnzymoPure™, ≥4 units/mg protein
生化机理	L-Amino acid oxidase 是一种黄蛋白，分子量为 130 kDa。它由两个分子量约为 70,000 Da 的不同亚基组成。每个全酶分子都有两个 FAD 分子。它是一种糖蛋白，含有约 2-5%的碳水化合物，包括硅铝酸。最佳 pH 值约为 7.5。在 38 ℃、pH 值为 7.5 的磷酸盐缓冲液中培养可使该酶可逆失活。L- 氨基酸氧化酶参与多种代谢途径，如丙氨酸和天冬氨酸代谢、蛋氨酸代谢、缬氨酸、亮氨酸和异亮氨酸降解、酪氨酸代谢、苯丙氨酸代谢、色氨酸代谢、苯丙氨酸、酪氨酸和色氨酸生物合成以及生物碱生物合成。
产品介绍	备注：请勿冷冻 Do not freeze！ One Unit oxidizes one micormole of L-leucine per minute at 25°C, pH 7.6. L-Amino Acid Oxidase is an oligomeric glycoprotein composed of unequal amounts of two different approximately 70 kDa subunits. Three electrophoretically different isozymes occur as different combinations of the two subunits. there are approximately two moles of FAD per mole of holo-enzyme. L-amino acid oxidase catalyzes the oxidative deamination of a number of L-amino acids. The enzyme is absolutely specific for L-isomers. The Aladdin product is prepared according to Wellner and Meister, JBC, 235, 2013, (1960) to the point just prior to crystallization.An aqueous solution with toluene added as a preservative. L-amino acid oxidase (LAAO) catalyzes the oxidative deamination of a number of L-amino acids, predominantly hydrophobic and aromatic L-amino acids. LAAO represents approximately 30% of the total venom of some snake species (Takatsuka et al. 2001). History LAAO was first discovered by Zeller and Maritz (Zeller and Maritz 1944, 1945). It was found to occur in almost all snake venoms and designated a flavoprotein in 1948 (Zeller 1948). LAAO was first prepared in crystalline form in 1958 by Wellner and Meister. In 1960, Wellner and Meister studied properties of the enzyme including prosthetic groups, electrophoretic fractions, stability, and pH dependence. In this study, they also isolated LAAO of Agkistrodon piscivorus piscivorus to compare it to that of C. adamanteus. Soon after, the enzyme mechanism was studied and further details of the mechanism were elucidated (Wellner and Meister 1961, and Massey and Curti 1967). The kinetics of the oxidase reaction were also investigated (Radd 1964, and Zeller et al. 1965). In the 1970s vinylglycine was determined to be a suicide substrate/inactivator of LAAO (Marcotte and Walsh 1976), and the effect of pH and competitive inhibitors was also studied (de Kok and Veeger 1968). LAAO of C. adamanteus was the first LAAO found to act as a bactericidal agent, a property that is still being studied today (Skarnes 1970, and Zuliani et al. 2009). The gene sequence was determined in 1998 by Raibekas and Massey. Recent work has involved using LAAOs to study apoptotic and cytotoxic effects (Stábeli et al. 2007), and LAAO is also being studied for its use as an anti-parasitic agent (Sant’Ana et al. 2008). Specificity LAAO is specific for L-isomers. Substrates are the L-isomers of leucine, isoleucine, norleucine, alpha-amino butyric acid, phenylalanine, tyrosine, tryptophan norvaline, methionine, histidine, and citrulline. Histidine and tyrosine cannot be determined in an L,D-mixture (Malmstadt and Hadjiioannov 1963). Methylene blue may be used as an electron acceptor. L-serine, threonine, aspartic acid, glutaric acid, lysine, and ornithine are deaminated only to a limited extent. LAAO is believed to contain three hydrophobic substrate binding sites, designated a, b, and c. Subsite a accommodates one methylene carbon, b two, and c three. An amino binding subsite is designated d (Tan et al. 1991). This model is used to explain why amino acids with branching at the second carbon are unable to accommodate into subsite a, and are oxidized slowly or not at all (Zuliani et al. 2009). Composition LAAOs are FAD-dependent enzymes and are usually homodimeric, binding glycoproteins with molecular masses of 110-150 kDA. Important residues identified in C. rhodostoma LAAO include Glu63, Arg71, and Glu457, which interact with the FAD molecule. The dimethylbenzene ring cofactor is surrounded by Ile374, Trp420, and Ile430; Lys326 coordinates a water molecule (Pawelek et al. 2000). These residues have been found to be conserved in the majority of snake venom LAAOs (Pawelek et al. 2000, and França et al. 2007). Molecular Characteristics LAAOs are widely distributed, being found in bacteria, fungi, green algae, plants, and snake venom. LAAOs of snake venom show a high degree of sequence homology, with conservation of at least 13 of the 24 N-terminal amino acids that are believed to be involved in substrate binding. (Zuliani et al. 2009). The N-terminal sequence contains a highly conserved beta-alpha-beta-fold domain involved in FAD binding (Du et al. 2002). Applications Purification and determination of certain amino acids (Nicholson and Kim 1975) Preparation of alpha-keto acid (Nicholson and Kim 1975) Assaying peptidase activity (Nicholson and Kim 1975, and Donlon and Fottrell 1971) Oxidation reactions Catalyst in supercritical CO2 (Findrik et al. 2005) Method The reaction velocity is determined in a peroxidase coupled system by measuring the increase in A436 resulting from the oxidation of L-leucine. One unit oxidizes one micromole of L-leucine per minute at 25°C and pH 7.6 under the specified conditions. Reagents 0.2 M Triethanolamine buffer pH 7.6 containing 0.1% L-leucine and 0.0065% o-dianisidine 1.0% Peroxidase: Dissolve Worthington Peroxidase (HPOD) at 10 mg/ml in water. Enzyme Dilute enzyme in reagent grade water to 0.05-0.2 units per milliliter. Procedure Adjust spectrophotometer to 436 nm and 25°C. Pipette into cuvettes 0.01 ml of 10 mg/ml peroxidase and 2.9 ml of 0.2 M triethanolamine-leucine-o-dianisidine mixture. Incubate in spectrophotometer at 25°C for 4-5 minutes to achieve temperature equilibration and record blank rate, if any. Add 0.1 ml of appropriately diluted enzyme and record increase in absorbance at 436 nm for 4-5 minutes. Calculate ΔA436 from the initial linear portion of the slope. Subtract blank rate if present. Calculation

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产品规格参数

浓度	≥4 units/mg protein
储存温度	2-8°C储存
运输条件	冰袋运输
CAS编号和信息	9000-89-9
酶学委员会编号	EC: 1.4.3.2
单位定义	Unit Defintion: One Unit oxidizes one micormole of L-leucine per minute at 25°C, pH 7.6
分子类型	酶

安全和危险性（GHS）

象形图	GHS06
信号词	Danger
危险声明	H300+H310+H330: 吞咽，皮肤接触或吸入会致命。
预防措施声明	P280: 戴防护手套/穿防护服/戴防护眼罩/戴防护面具。 P301+P310: 如误吞咽：立即呼叫急救中心/医生。 P264: 处理后要彻底洗手。 P260: 不要吸入灰尘/烟雾/气体/雾/蒸汽/喷雾。 P284: 如果通风不良，请佩戴呼吸防护装置。 P302+P350: 如果皮肤接触：用大量肥皂和水轻轻清洗。
WGK Germany	3

SDS英文版

技术规格说明书

Enzymatic Activity	≥4（units/mg）

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找到6个结果

批号(Lot Number)	证书类型	日期	货号
H2127111	分析证书	23-03-15	A128538
J2022052	分析证书	22-07-09	A128538
J2022051	分析证书	22-07-09	A128538
H2127550	分析证书	22-06-22	A128538
H2127094	分析证书	22-06-22	A128538
H2127124	分析证书	22-06-22	A128538

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货号 (SKU)	包装规格	是否现货	价格	数量
A128538-2mg	2mg	期货
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L-氨基酸氧化酶来源于东部菱背响尾蛇毒液

库存信息

库存信息

基本描述

AI解读

产品规格参数

安全和危险性（GHS）

技术规格说明书

质检证书（CoA,COO,BSE/TSE 和分析图谱)

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溶液计算器

摩尔浓度计算器

稀释计算器

复溶计算器

L-氨基酸氧化酶 来源于东部菱背响尾蛇毒液

库存信息

库存信息

基本描述

AI解读

产品规格参数

安全和危险性（GHS）

技术规格说明书

质检证书（CoA,COO,BSE/TSE 和分析图谱)

相关技术文章

溶液计算器

摩尔浓度计算器

稀释计算器

复溶计算器

L-氨基酸氧化酶来源于东部菱背响尾蛇毒液