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Amino Acid Sequence Homology between HLA‐A,B,C Antigens, β 2 ‐Microglobulin and Immunoglobulins
Author(s) -
TRÄGÅRDH L.,
WIMAN K.,
RASK L.,
PETERSON P. A.
Publication year - 1978
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1978.tb00557.x
Subject(s) - peptide sequence , beta 2 microglobulin , chemistry , antibody , peptide , papain , cysteine , amino acid , homology (biology) , biochemistry , microbiology and biotechnology , epitope , antigen , immunoglobulin heavy chain , stereochemistry , biology , genetics , enzyme , gene , immunology
Papain‐solubilized HLA‐A. B.C antigen heavy chains have been cleaved by combined acid and CNBr treatment to yield three large fragments. A 14,000‐dalton peptide comprises the NH 2‐ terminal portion of the molecule, less a five‐membered peptide The 14,000‐dalton fragment is followed in the linear sequence by a 9000‐dalton peptide connected through an aspartyl‐prolyl bond to the COOH‐terminal 11,000‐dalton fragment. The 9000‐ and 11,000‐dalton fragments contain disulphide bridges that are immunoglobulin‐like inasmuch as they encompass some fifty‐live lo sixty amino acid residues. The NH 2 ‐terminal portion of the HLA antigen heavy chain is devoid of cysteine. NH 2 ‐terminal amino acid sequence analyses do not reveal homologies between the 14.000‐ and 9000‐dalton fragments. β 2 ‐microglobulin, and the constant immunoglobulin domains. However, the NH 2 ‐terminal sequence of the 11,000‐dalton fragment is as homologous to β 2 ‐microglobulin and the constant immunoglobulin domains as they are to one another.