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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关于此项目
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
此项目有
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
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)
Carlos Martinez-Fleites et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 65(Pt 10), 963-966 (2009-10-24)
The crystal structures of truncated forms of the Streptococcus pyogenes phage-encoded hyaluronate lyases HylP2 and HylP3 were determined by molecular replacement to 1.6 and 1.9 A resolution, respectively. The truncated forms crystallized in a hexagonal space group, forming a trimer
S-C Wu et al.
Journal of food science, 72(8), S618-S621 (2007-11-13)
The effects of particle size changes by micronization on the intestinal health-promotion ability of orange insoluble fiber fraction (IFF) were investigated in a hamster model by feeding 3 diets, which contained unmicronized IFF (control), jet-milled IFF, and high-pressure micronized IFF
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