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：1983
卷号：80
期号：6
页码：1698-1702
DOI：10.1073/pnas.80.6.1698
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The human erythrocyte receptor for the major activation fragments of the third and fourth components of complement (HuE-C3bR) was isolated from individual donors. Erythrocytes were surface labeled with 125I and solubilized in Nonidet P-40.HuE-C3bR was purified by using C3-Sepharose affinity chromatography and analyzed by autoradiography of NaDodSO4/polyacrylamide gels. Three distinct receptor patterns were demonstrated. Type a had a single major band with Mr of 190,000, type b had a single major band with Mr of 220,000, and type c had two major bands of Mr 190,000 and 220,000. In all three types, a minor band accounting for less than 25% of the total radioactivity was usually observed at a Mr 15,000 greater than that of each major band. Identical autoradiographic patterns were obtained by affinity chromatography using methylamine-inactivated C4-Sepharose or by immunoprecipitation of solubilized membranes with a monoclonal antibody against HuE-C3bR. All three types were distinct after reduction and alkylation, although the apparent Mr uniformly increased by approximately equal to 30,000. Characterization of HuE-C3bR types in 33 unrelated individuals demonstrated that 23 had type a, 1 had type b, and 9 had type c. Family studies provide evidence for transmission by two codominant alleles. Thus, in the normal population two alleles appear to control expression of HuE-C3bR phenotypes and account for the polymorphism of this integral membrane glycoprotein.
