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HL-A antigens comprising 11 different antigenic specificities were isolated after papain solubilization of spleen-cell membrane constituents. During the entire purification procedure, beta(2)-microglobulin appeared together with the HL-A antigens. The highly purified antigens were composed of two polypeptide chains. The large subunit carried the antigenic specificity whereas the small polypeptide chain was very similar, if not identical, to beta(2)-microglobulin. The two HL-A antigen polypeptide chains were held together by noncovalent interactions only, and beta(2)-microglobulin, isolated from urine, could replace the small subunit in forming a complex with the large polypeptide chain. The topographical relationship in the cell membrane between beta(2)-microglobulin and the large HL-A antigen polypeptide chain is unknown. The two polypeptide chains may be fortuitously bound as a result of the solubilization procedure.
P A Peterson, and
L Rask, and
J B Lindblom
May 1973,
Proceedings of the National Academy of Sciences of the United States of America,
P A Peterson, and
L Rask, and
J B Lindblom
April 1975,
Proceedings of the National Academy of Sciences of the United States of America,
P A Peterson, and
L Rask, and
J B Lindblom
July 1974,
Transplantation,
P A Peterson, and
L Rask, and
J B Lindblom
June 1975,
Transplantation proceedings,
P A Peterson, and
L Rask, and
J B Lindblom
January 1974,
Immunology,
P A Peterson, and
L Rask, and
J B Lindblom
January 1980,
Scandinavian journal of immunology,
P A Peterson, and
L Rask, and
J B Lindblom
January 1973,
Immunology,
P A Peterson, and
L Rask, and
J B Lindblom
May 1974,
The Journal of biological chemistry,
P A Peterson, and
L Rask, and
J B Lindblom
December 1973,
Science (New York, N.Y.),
P A Peterson, and
L Rask, and
J B Lindblom
August 1978,
Transplantation,
