文章基本信息

标题：Evolutionary relationship between immunoglobulins and transplantation antigens
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作者：P A Peterson ; L Rask ; K Sege 等
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：1975
卷号：72
期号：4
页码：1612-1616
DOI：10.1073/pnas.72.4.1612
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The major human and murine histocompatibility antigens are tetrameric molecules with an apparent molecular weight of about 130,000. They are composed of two types of polypeptide chains. The two light chains, previously identified as beta2-microglobulins, are bound to the two heavy, alloantigenic HL-A or H-2 polypeptide chains by noncovalent interactions only. The heavy chains are held together by disulfide bridge(s) located in the part of the molecule that is attached to the cell membrane. By limited proteolysis of the histocompatibility antigens evidence was obtained suggesting that the heavy chain may consist of three compact domains connected by more extended stretches of polypeptide chain. Each domain appeared to contain a single disulfide bride encompassing about 60 to 70 amino-acid residues. Staphylococcus aureus protein A is known to bind exclusively to the Fe region of immunoglobulin G. It was, however, observed that protein A interacts in a similar way with the H-2 antigen heavy chain. This observation, together withthe homology of the primary structure of beta2-microglobulin to immunoglobulin G, the tetrameric structure of the alloantigens, the ogranizations of the heavy polypeptide chain into compact domains, and the presence of a single, immunoglobulin-like disulfide loop in each domain, establishes a close similarity in structure between histocompatibility antigens and immunoglobulins. The similarity in structural features suggests a common evolutionary origin of the two types of molecules.