Further structural studies of the heavy chain of HLA antigens and its similarity to immunoglobulins.
AUTOR(ES)
Terhorst, C
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=431819Documentos Relacionados
- The amino acid sequence and gene organization of the heavy chain of the HLA-DR antigen: homology to immunoglobulins.
- A transgenic mouse that expresses a diversity of human sequence heavy and light chain immunoglobulins.
- Evolutionary and structural influences on light chain constant (CL) region of human and mouse immunoglobulins.
- Structural implications of sequence variability in immunoglobulins.
- Immunoglobulins.