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：1
页码：255-258
DOI：10.1073/pnas.80.1.255
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A chemically synthesized dodecapeptide (Asp-Ala-Ala-Ser-Pro-Arg-Glu-Glu-Pro-Arg-Ala-Pro), consisting of residues 39 through 50 of the HLA-B7 heavy chain sequence and containing a highly hydrophilic hexapeptide segment (Pro-Arg-Glu-Glu-Pro-Arg), induced antibodies that bound specifically to free HLA-A, and HLA-B heavy chains and to the soluble dodecapeptide. Although these antibodies reacted with free HLA-A,B heavy chains in blots on nitrocellulose, they failed to immunoprecipitate the HLA-A,B-beta 2-microglobulin antigen complex solubilized from human lymphoblastoid cells by nonionic detergents. These observations suggest that the physical characteristics of this particular soluble hydrophilic dodecapeptide may closely resemble nonallotypic determinants expressed by free HLA-A,B heavy chains and that such antigenic sites may be modified by conformational changes in the native HLA-A,B heavy chain-beta 2-microglobulin complex.
