Human milk-fat globule membrane derived mucin is a disulfide-linked heteromer.
Human milk-fat globule membrane derived mucin is a disulfide-linked heteromer.
复制标题
人乳脂肪球膜衍生的粘蛋白是一种二硫键连接的异聚体。
DOI：
10.1016/0006-291x(89)92745-9
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发表时间：
1989
影响因子：
3.1
通讯作者：
Ceriani,RL
中科院分区：
文献类型：
--
作者：
Duwe,AK;Ceriani,RL
The human milk-fat globule membrane (HMFG) contains a number of antigens also expressed on breast tumors. The dominant antigens are a mucin of MW > 400,000 and a group of antigens of MW 67,000–70,000. The mucin was separated with monoclonal antibodies against HMFG and a MW 70,000 doublet was found to be associated with the mucin under non-reducing conditions, the latter identifiable by another set of monoclonal antibodies. Immunoprecipitation of the mucin and analysis of the precipitated material using Western blots and identification of transferred material with monoclonal antibodies demonstrated that the MW 70,000 protein and the mucin were co-precipitated and linked by reducible disulfide bonds. Treatment with detergents, protein-dissociating agents and glycosidases did not release the component from the mucin. Mucins in HMFG membrane and breast tumor cells may be associated therefore to disulfide-linked linker proteins similar to those described for intestinal and gastric mucins, that would co-purify with the mucin under non-reducing conditions.
