A glycolipid and its associated proteins: evidence by crosslinking of human erythrocyte surface components
A glycolipid and its associated proteins: evidence by crosslinking of human erythrocyte surface components
复制标题
糖脂及其相关蛋白质：人红细胞表面成分交联的证据
DOI：
10.1016/0014-5793(80)80194-3
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发表时间：
1980
期刊：
影响因子：
3.5
通讯作者：
T. Ji
中科院分区：
文献类型：
--
作者：
C. Lingwood;S. Hakomori;T. Ji
1. Introduction~ lycosphingolipids function as antigens [I], receptors [2] and possibly regulators of cell proliferation and interaction 131. They are chemically well defined, but they may represent only a part of the complex membrane machinery through which functions are achieved. Therefore, putative membrane proteins that may specifically interact with glycolipids have been postulated [4]. Their presence has been indicated by association of the specific membrane protein to a specific affinity glycolipid-glass column although the protein was not eluted nor isolated 151. Two amphipathic low molecular weight (~ 4000) proteins have been isolated from ethanol and chloroform-methanol extracts of bovine erythrocytes that have some affinity to gangiioside (gangliophilin) and one of them displayed a strong Paul-Bunnell antigen activity [6]. The topology and organization of gIycoIipids and membrane proteins is now studied by heterobifunctional crosslinking reagents introduced in 171. A large variety of crosslinking reagents have been used to study the arrangement and organization of proteins within cell membranes [S-lo]. Methyl-4-azidobenzoimidate (MABI) terminates in a light-sensitive arylazido group which is coupled to an imidoester function whichAbbreviations: MABI, methyWazidobenzoimide: PMSF, pbenylmethylsulfonyl~ uo~ de; PBS, phosphate buffered saline (0.14 M NaCl, 2.6 mM KC& 8 mM Na, HPO,, 1.5 mM KH, PO, pH adjusted as indicated): RBC, red blood cells; globoside, a major glycolipid of human RBC membrane with a structure GalNAcpl-3 Ga~ ffl~ 4Gal~ l~ 4Gl~ ljlCer[12]
