56177
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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Specific activity:
≥8.0 units/mg protein (5.0-15.0 mg/mL)
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
form
liquid
specific activity
≥8.0 units/mg protein (5.0-15.0 mg/mL)
storage temp.
2-8°C
Biochem/physiol Actions
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。
Physical form
硫酸铵悬浮液
Other Notes
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。
存储类别
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
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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)
Substrate specificity of the heparin lyases from Flavobacterium heparinum.
Desai, U.R., et al.
Archives of Biochemistry and Biophysics, 461-468 (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
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.
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
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