跳转至内容
Merck
CN

L6150

赖氨酸氧化酶 来源于绿色木霉

lyophilized powder, ≥20 units/mg protein

别名:

L -赖氨酸:氧氧化还原酶(脱氨)

登录 查看组织和合同定价。

选择尺寸

变更视图

关于此项目

化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥20 units/mg protein
Biological source:
fungus (Trichoderma viride)
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助

biological source

fungus (Trichoderma viride)

Quality Level

form

lyophilized powder

specific activity

≥20 units/mg protein

mol wt

112 kDa

composition

Protein, 5-20%

storage temp.

2-8°C

General description

赖氨酸氧化酶(来自绿色木霉)是一种分子量为112kDa的同型二聚体黄素酶。在65°C下稳定,对L-赖氨酸具有高度选择性。它由FAD结合、底物结合和螺旋结构域组成,具有明显的活性部位通道。

Application

赖氨酸氧化酶(来自绿色木霉)已用于制备生物发光芯片。

Biochem/physiol Actions

赖氨酸氧化酶(来自绿色木霉)通过催化L-赖氨酸的氧化脱氨形成α-酮基-ε-氨基己酸。它在白血病细胞中表现抗癌能力,也是鳞状细胞、成纤维细胞、卵巢和胃癌的肿瘤抑制剂。赖氨酸氧化酶在结缔组织结构完整性和胚胎发育中起重要作用。

Physical form

含有磷酸盐缓冲盐和稳定剂

Other Notes

一个单元在 37°C,pH 8.0 的条件下催化 L-赖氨酸每分钟生成 1 μmol 的 6-氨基-2-氧代己酸。

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

常规特殊物品

此项目有


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

没有发现合适的版本?

如果您需要特殊版本,可通过批号或批次号查找具体证书。

已有该产品?

在文件库中查找您最近购买产品的文档。

访问文档库

I P Smirnova et al.
Voprosy meditsinskoi khimii, 46(4), 384-387 (2000-11-15)
The ability of protein isolated from (Trichoderma Rifai) and azydothymidine to inhibit the reproduction of HIV-virus was compared. The obtained experimental data have verified that Trichoderma Rifai protein is a promising human immunodeficiency virus (HIV) inhibitor.
O S Zhukova et al.
Voprosy meditsinskoi khimii, 47(6), 588-592 (2002-04-03)
The conjugates of L-lysine alpha-oxidase and monoclonal antibodies ICO-80 towards CD-5 receptor were produced using glutaraldehyde. The cytotoxic effect of conjugates on Yurkat cells line appeared to be lower in comparison with the native enzyme. Negligible decrease of conjugate biological
Seiji Okazaki et al.
Journal of biochemistry, 154(3), 233-236 (2013-08-03)
We have determined the x-ray crystal structure of L-lysine ε-oxidase from Marinomonas mediterranea in its native and L-lysine-complex forms at 1.94- and 1.99-Å resolution, respectively. In the native enzyme, electron densities clearly indicate the presence of cysteine tryptophylquinone (CTQ) previously
Jedidah W Danson et al.
Analytical biochemistry, 303(2), 120-130 (2002-04-13)
A new assay for l-lysine alpha-oxidase is described. In this assay, the oxidized product generated from l-lysine is reacted with semicarbazide to form alpha-keto-epsilon-aminocaproate semicarbazone. Formation of the alpha-keto acid semicarbazone is continuously monitored spectrophotometrically at 248 nm (epsilon 10,160
E V Lukasheva et al.
Voprosy meditsinskoi khimii, 43(6), 566-575 (1998-03-21)
The goal of the present study was the development of the optimal method of co-immobilization of two enzymes: L-lysine alpha-oxidase from Trichoderma sp. and horseradish peroxidase. Commercial nitrocellulose, nylon and N+ nylon membranes were used as carriers. The immobilization was

相关内容

Product Information Sheet

全球贸易项目编号

货号GTIN
L6150-25UN04061833958650

我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.

联系客户支持