Further structural studies of the heavy chain of HLA antigens and its similarity to immunoglobulins.
- 1 September 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (9), 4002-4006
- https://doi.org/10.1073/pnas.74.9.4002
Abstract
The papain-solubilized fragment of the heavy chain of HLA-B7, which is the NH2-terminal part of the whole polypeptide chain, can be divided into three regions by mild acid and cyanogen bromide cleavages. The first 100 amino acids terminating in a methionine residue contain the carbohydrate moiety; this segment is followed by two others of molecular weights 9,999 and 13,000, each containing an intrachain disulfide bridge. The two intrachain disulfide bridges are separated by a stretch of amino acids containing an acid-labile aspartyl-prolHLA-2, A28, and AW25 contain this acid-labile peptide bond in their larger subunit. Sequencing from the acid cleavage site of HLA-7 through the third half-cystine revealed consideralbe homology with amino acid sequences around a half-cystine in immunoglobulin variable regions.Keywords
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