所有图片(1)

77160

Sigma-Aldrich

胃蛋白酶 来源于猪胃粘膜

powder, slightly beige, ≥500 U/mg

别名:
胃液素 来源于猪胃, 胃蛋白酶 A
CAS号:
EC 号:
MDL编号:
eCl@ss:
42010127
NACRES:
NA.54

形式

powder

specific activity

≥500 U/mg

分子量

35 kDa

颜色

slightly beige

UniProt登记号

储存温度

2-8°C

Gene Information

正在寻找类似产品? Visit 产品对比指南

应用

胃蛋白酶切割可用于产生抗体的F(ab′)2 片段。有关胃蛋白酶的更多信息,请访问 www.sigma-aldrich.com/enzymeexplorer

生化/生理作用

优先裂解:P1 和 P1′ 位的疏水性和芳族残基。降解胰岛素 β 链中的 Phe-Val、Gln-His、Glu-Ala、Ala-Leu、Leu-Tyr、Tyr-Leu、Gly-Phe、Phe-Phe 和 Phe-Tyr 键

单位定义

1 个单位对应于在 pH 2.0 和 37℃ 下每分钟使 280 nm 处的吸光度增加 0.001 的酶量(血红蛋白,目录号 51290,作为底物);上述 15,000 吸光度单位相当于约1 个 Bergmeyer 单位。一个Bergmeyer单位是在pH2.0和37℃下水解1 μmol乙酰基-L-苯基-3,5-二碘-L-酪氨酸的酶量。

分析说明

最适pH值为2-4。在4 M尿素和3 M盐酸胍中可保持活性。在60°C时稳定。胃蛋白酶在pH 8.0-8.5下发生不可逆灭活。

其他说明

可能适用相应的销售限制。
多肽合成,综述。

象形图

Exclamation markHealth hazard

警示用语:

Danger

危险分类

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

靶器官

Respiratory system

储存分类代码

11 - Combustible Solids

WGK

WGK 1

闪点(F)

Not applicable

闪点(C)

Not applicable

个人防护装备

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

分析证书

原产地证书 (CofO)

M.P. Bemquerer et al.
Biomedica Biochimica Acta, 50 (1991)
C A Abdel Malak et al.
International journal of peptide and protein research, 41(2), 97-101 (1993-02-01)
Swine pepsin at pH 5 efficiently catalyzes a condensation between Z-Ala-Ala-Phe-OH and p-nitroanilides of Leu, Phe, Val, Ala and Arg that leads to formation of corresponding benzyloxycarbonyl-tetrapeptide p-nitroanilides with yields of 70-90%. These reactions are complicated by co-precipitation of pepsin
J.S. Fruton
Carlsberg Research Communications, 49, 41-41 (1984)
Benoît Stijlemans et al.
PLoS pathogens, 7(6), e1002072-e1002072 (2011-06-24)
The African trypanosome Trypanosoma brucei, which persists within the bloodstream of the mammalian host, has evolved potent mechanisms for immune evasion. Specifically, antigenic variation of the variant-specific surface glycoprotein (VSG) and a highly active endocytosis and recycling of the surface
Dragana Stanic-Vucinic et al.
Molecular nutrition & food research, 56(12), 1894-1905 (2012-10-16)
The aim of this work was to investigate the effects of high-intensity ultrasound (sonication), on the structure and allergenicity of the major cow's milk allergen, beta-lactoglobulin (BLG). Structural changes upon sonication of BLG were monitored by circular dichroism spectroscopy, tryptophan

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.

联系技术服务部门