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Published February 1, 1976 | public
Journal Article Open

Structure and evolution of transplantation antigens: Partial amino-acid sequences of H-2K and H-2D alloantigens


Techniques for the amino acid sequence analysis of subnanomole quantities of polypeptides have been applied to characterize β2-microglobulin and transplantation antigens of the mouse isolated from spleen cells by indirect immunoprecipitation. Eleven residues were identified throughout the NH2-terminal 27 residues of the β2-microglobulin; all were identical to residues seen at the corresponding positions of β2-microglobulins from other species. Two K and two D transplantation antigens were examined and the following generalizations emerged from the limited partial amino-acid sequence data: (1) the K and D molecules are homologous to one another; (2) they do not show amino acid sequence homology with immunoglobulins; (3) the two K and two D molecules differ from one another by multiple amino acid substitutions; and (4) the K molecules as a class cannot be distinguished from the D molecules as a class. The genetic and evolutionary implications of these observations are discussed.

Additional Information

© 1976 by the National Academy of Sciences. Communicated by Ray D. Owen, November 24, 1975. This work was supported by grants from the National Science Foundation and the National Institutes of Health. J.S. has an Established Investigatorship Award from the American Heart Association. L.H. has a National Institutes of Health Research Career Development Award. We thank Paul Morand for his outstanding technical assistance.


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