Ineraction of GM2 Activator Protein with Glycosphingolipids
Ineraction of GM2 Activator Protein with Glycosphingolipids
复制标题
GM2 激活蛋白与鞘糖脂的相互作用
DOI：
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Yu
中科院分区：
文献类型：
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作者：
Su;Y. Hama;Yu
GM2激活蛋白是一种蛋白辅因子，可分别刺激β-氨基己糖苷酶A和唾液酸酶对GM2中的GalNAc和NeuAc的水解。为了了解GM2激活剂的作用机制，自从纯化的GM2激活剂问世以来，该蛋白与GM2和/或β-氨基己糖苷酶A的相互作用一直是人们感兴趣的主题。采用超速离心法、等电聚焦、聚丙烯酰胺凝胶电泳法、凝胶过滤、薄层层析、荧光去猝灭等多种技术，研究了GM2激活剂与不同类型鞘糖脂的结合和亲和力。人们普遍认为，GM2激活剂与酶的结合一定很弱，因为它们很容易分离，GM2激活剂蛋白是一种蛋白质辅因子，分别刺激β-己糖氨酸酶A和唾液酸酶对GM2中的GalNAc和NeuAc的水解。为了了解GM2激活剂的作用机制，自从纯化的GM2激活剂问世以来，该蛋白与GM2和/或β-氨基己糖苷酶A的相互作用一直是人们感兴趣的主题。采用超速离心法、等电聚焦、聚丙烯酰胺凝胶电泳法、凝胶过滤、薄层层析、荧光去猝灭等多种技术，研究了GM2激活剂与不同类型鞘糖脂的结合和亲和力。人们普遍认为GM2激活剂必须与酶有很弱的结合，因为它们很容易通过凝胶过滤分离出来。因此，GM2和GM2激活剂的相互作用一直是研究的重点。虽然一些方法检测到GM2激活剂与GM2的优先结合，但也发现GM2激活剂还与其他糖鞘磷脂结合。从含有激活剂蛋白和混合糖鞘糖脂的孵育混合物中分离出仅由GM2激活剂和GM2组成的特异性复合体尚未成功进行。
GM2 activator protein is a protein cofactor that stimulates the hydrolysis of the GalNAc and the NeuAc in GM2 by β-hexosaminidase A and sialidase, respectively. To understand the mechanism of action of GM2 activator, the interaction of this protein with GM2 and/or β-hexosaminidase A has been the subject of interest since the purified GM2 activator became available. Numerous techniques including ultracentrifugation, isoelectric focusing, polyacrylamide gel electrophoresis, gel filtration, thin layer chromatogram overlay, and fluorescence dequenching assay have been used to investigate the binding and the affinity of GM2 activator to various glycosphingolipids. It has been generally accepted that GM2 activator must have a very weak binding with the enzyme, because they can be easily separated GM2 activator protein is a protein cofactor that stimulates the hydrolysis of the GalNAc and the NeuAc in GM2 by β-hexosaminidase A and sialidase, respectively. To understand the mechanism of action of GM2 activator, the interaction of this protein with GM2 and/or β-hexosaminidase A has been the subject of interest since the purified GM2 activator became available. Numerous techniques including ultracentrifugation, isoelectric focusing, polyacrylamide gel electrophoresis, gel filtration, thin layer chromatogram overlay, and fluorescence dequenching assay have been used to investigate the binding and the affinity of GM2 activator to various glycosphingolipids. It has been generally accepted that GM2 activator must have a very weak binding with the enzyme, because they can be easily separated from each other by gel filtration. Therefore, the interaction of GM2 and GM2 activator has been the focus for most of the study. Although preferential association of GM2 activator with GM2 was detected by some methods, GM2 activator was found also to bind other glycosphingolipids. Isolation of the specific complex that consists of only GM2 activator and GM2 from an incubation mixture containing the activator protein and mixed glycosphingo-lipids has not been successfully carried out.
小鼠 GM2 激活蛋白和 β-N-乙酰己糖胺酶 A 和 B 的特异性。GM2 分解代谢与人类对应物的异同。
DOI：
10.1074/jbc.273.1.66
发表时间：
1998
期刊：
The Journal of biological chemistry
影响因子：
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作者：
Yuziuk,JA;Bertoni,C;Beccari,T;Orlacchio,A;Wu,YY;Li,SC;Li,YT
通讯作者：
Li,YT