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An approach to amino acid sequence analysis of transplantation antigens

Abstract

THE major histocompatibility complex of the mouse, known as the H-2 locus, represents the prime barrier against successful tissue transplants1 and controls the expression of many cell surface alloantigens which are serologically detectable2,3. It may be subdivided by recombinational analysis into four major regions known as K, D, Ir and Ss (ref. 4). The Ss region controls the quantitative expression of a serum protein5. The Ir region controls immune responsiveness of mice to a variety of synthetic and natural antigens6,7, and the expression of multiple cell surface proteins, some of which may be distinguished by molecular weight8,9. The K and D regions both control the expression of distinct cell surface glycoproteins (molecular weight 47,000), which are non-covalently associated with a small molecular weight (11,500) component10–11. Because the native molecules are hydrophobic proteins present on the cell surfaces in small quantities, it is necessary to use unusual procedures for their isolation and chemical characterisation. We have, therefore, used indirect immunoprecipitation and sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis (PAGE) for the isolation and subsequent amino acid sequence analysis of both molecular weight components.

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SILVER, J., HOOD, L. An approach to amino acid sequence analysis of transplantation antigens. Nature 256, 63–64 (1975). https://doi.org/10.1038/256063a0

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