Abstract
Three preparations of purified papain-solublized HL-A antigens have been radiolabeled by reductive methylation using formaldehyde and potassium boro[3H]hydride, and their reaction with specific HL-A antisera has been investigated. Greater than 99 percent of the radioactivity in the [3H]HL-A2 preparation could be complexed with several HL-A2 antisera, but not with specificity controls. The other two preparations, which contained mixtures of HL-A antigenic specificities (HL-A7,12 an HL-A3,W25;12,27), showed 63 per cent and 70 per cent complex formation with mixtures of the appropriate HL-A antisera. The N-terminal amino acid of both subunits has been determined for the three HL-A antigen preparations. In all cases the only detectable N-terminal amino acids were isoleucine for the small subunits, beta-2-microblogulin, and glycine for the larger subunit.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 3:05 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 11:03 a.m.) |
Indexed | 1 year, 9 months ago (Nov. 10, 2023, 7:36 p.m.) |
Issued | 50 years, 5 months ago (April 1, 1975) |
Published | 50 years, 5 months ago (April 1, 1975) |
Published Online | 50 years, 5 months ago (April 1, 1975) |
Published Print | 50 years, 5 months ago (April 1, 1975) |
@article{Parham_1975, title={Immunological and chemical purity of papain-solubilized HL-A antigens.}, volume={72}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.72.4.1594}, DOI={10.1073/pnas.72.4.1594}, number={4}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Parham, P and Terhorst, C and Herrmann, H and Humphreys, R E and Waterfield, M D and Strominger, J L}, year={1975}, month=apr, pages={1594–1598} }