期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1977
卷号：74
期号：10
页码：4591-4594
DOI：10.1073/pnas.74.10.4591
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A purified human monoclonal IgM({kappa}) (cold agglutinin MKV) has been characterized as both a cold agglutinin and a cryoglobulin. Since its reactivity with human erythrocytes but not with dog erythrocytes is reduced by treatment of the cells with ficin and its reactivity with both is abolished by treatment of the cells with neuraminidase, it has by definition Pr2 specificity [Roelcke, D. (1974) Clin. Immunol. Immunopath. 2, 266-280]. Presumably, the membrane receptors for cold agglutinin MKV are sialic acid-containing glycoproteins in human cells and sialic acid-containing glycolipids in dog cells. Agglutination of erythrocytes is specifically inhibited by II3-N-acetylneuraminosyllactosylceramide (GM3) and N-acetylneuraminosylparagloboside but not by their N-glycolylneuraminosyl forms or by lactosylceramide or paragloboside, and the reactivity of neuraminidase-treated cells can be restored by allowing them to absorb either GM3 or N-acetylneuraminosylparagloboside. When large amounts of ganglioside are absorbed, the cells are agglutinated not only in the cold, but also at 37{degrees
关键词：receptors ; glycoproteins ; glycolipids ; erythrocytes ; blood groups
