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 beta2-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 beta2-microglobulin; all were identical to residues seen at the corresponding positions of beta2-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.
D000595:Amino Acid Sequence; D000818:Animals; D001609:Beta-Globulins / Q000032:analysis*; D005075:Biological Evolution; D002874:Chromosome Mapping; D004285:Dogs / Q000276:immunology; D006649:Histocompatibility Antigens / Q000032:analysis* / Q000302:isolation & purification; D006801:Humans; D051379:Mice / Q000276:immunology; D013045:Species Specificity; D013154:Spleen / Q000276:immunology; D001613:beta 2-Microglobulin / Q000032:analysis*
D001609:Beta-Globulins; D006649:Histocompatibility Antigens; D001613:beta 2-Microglobulin