By use of single internal radiolabels, 17 of the NH2 terminal 27 amino acids of the murine H2 Kb molecule have been assigned. When the amino acid sequence is compared to that of the murine H 2Kk molecule, there is a minimum of six amino acid differences in 19 positions. This high degree of structural diversity confirms, at the level of amino acid sequence, the known polymorphism of the murine H 2 complex. Significant primary structural homology is evident when the murine H 2Kk and H 2Kb sequences are compared to the recently reported partial amino acid sequences of human transplantation antigens. There is modest homology with β2 microglobulin and immunoglobulins, but the available sequence information is insufficient for a satisfactory evaluation of its significance.
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