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Merck
CN

56177

Sigma-Aldrich

透明质酸裂解酶 来源于化脓链球菌

≥8.0 units/mg protein (5.0-15.0 mg/mL)

别名:

透明质酸酶 来源于化脓链球菌

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关于此项目

CAS Number:
MDL编号:
UNSPSC代码:
12352204
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重组

expressed in E. coli

表单

liquid

比活

≥8.0 units/mg protein (5.0-15.0 mg/mL)

储存温度

2-8°C

生化/生理作用

透明质酸裂解酶通过消除反应破坏糖苷键,从而降解透明质酸,并产生不饱和二糖产物。它对化脓链球菌产生毒素和蛋白质扩散具有重要作用。
透明质酸裂解酶通过消除反应破坏糖苷键,从而降解透明质酸,并产生不饱和二糖产物。它对化脓链球菌产生毒素和蛋白质扩散具有重要作用。

外形

硫酸铵悬浮液

其他说明

1U 对应于在 pH6.0 和 37℃ 下每分钟从透明质酸(货号 53747)释放 1 μmol 不饱和二糖的酶量。

储存分类代码

12 - Non Combustible Liquids

WGK

WGK 2

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

新产品

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Structural studies on the bacterial lyase-resistant tetrasaccharides derived from the antithrombin III-binding site of porcine intestinal heparin.
Yamada, S., et al.
The Journal of Biological Chemistry, 4780-4787 (1993)
R J Linhardt et al.
Applied biochemistry and biotechnology, 12(2), 135-176 (1986-04-01)
Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products. Acidic
Substrate specificity of the heparin lyases from Flavobacterium heparinum.
Desai, U.R., et al.
Archives of Biochemistry and Biophysics, 461-468 (1993)
Md Sohail Akhtar et al.
Biochemical and biophysical research communications, 353(2), 286-292 (2006-12-26)
Hyaluronate lyases from Streptococcus pneumoniae (SpnHL) and Streptococcus agalactiae (SagHL) are composed of four domains; N-terminal domain, spacer domain, alpha-domain and C-terminal domain, which are connected through peptide linkers. We have earlier shown that the recombinant alpha- and C-terminal domains
Harshad V Joshi et al.
Proteins, 76(1), 30-46 (2008-12-18)
Hyaluronan lyase (Hyal) is a surface enzyme occurring in many bacterial organisms including members of Streptococcus species. Streptococcal Hyal primarily degrades hyaluronan-substrate (HA) of the extracellular matrix. This degradation appears to facilitate the spread of this bacterium throughout host tissues.

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