Receptor affinity purification of a lipid-binding adhesin from Helicobacter pylori
Receptor affinity purification of a lipid-binding adhesin from Helicobacter pylori
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幽门螺杆菌脂质结合粘附素的受体亲和纯化
DOI：
10.1128/iai.61.6.2474-2478.1993
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发表时间：
1993
影响因子：
3.1
通讯作者：
M. Huesca
中科院分区：
文献类型：
--
作者：
C. Lingwood;G. Wasfy;H. Han;M. Huesca
我们以前的工作表明，幽门螺杆菌在体外特异性识别神经节四糖基神经酰胺、神经节三糖基神经酰胺和磷脂酰乙醇胺。铜绿假单胞菌的外切酶S也具有这种结合特异性，抗这种粘附素的单克隆抗体可阻止H的附着。pylori的脂质受体。我们现在报告使用一种新的，通用的亲和基质纯化63 kDa的外切酶S样粘附素从H。幽门螺杆菌，其负责该生物体的脂质结合特异性。
Our previous work has shown that Helicobacter pylori specifically recognizes gangliotetraosylceramide, gangliotriaosylceramide, and phosphatidylethanolamine in vitro. This binding specificity is shared by exoenzyme S from Pseudomonas aeruginosa, and monoclonal antibodies against this adhesin prevent the attachment of H. pylori to its lipid receptors. We now report the use of a novel, versatile affinity matrix to purify a 63-kDa exoenzyme S-like adhesin from H. pylori which is responsible for the lipid-binding specificity of this organism.
影响因子：
158.5
作者：
PARSONNET, J;FRIEDMAN, GD;SIBLEY, RK
通讯作者：
SIBLEY, RK
影响因子：
158.5
作者：
NOMURA, A;STEMMERMANN, GN;BLASER, MJ
通讯作者：
BLASER, MJ