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- Title
Amino Acid Sequence Homology between HLA--A,B,C Antigens, β<sub>2</sub>--Microglobulin and Immunoglobulins.
- Authors
Trägärdh, L.; Wiman, K.; Rask, L.; Peterson, P.A.
- Abstract
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 NH2-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-five to sixty amino acid residues. The NH2-terminal portion of the HLA antigen heavy chain is devoid of cysteine. NH2-terminal amino acid sequence analyses do not reveal homologies between the 14,000- and 9000-dalton fragments, β2-microglobulin, and the constant immunoglobulin domains. However, the NH2-terminal sequence of the 11,000-dalton fragment is as homologous to β2-microglobulin and the constant immunoglobulin domains as they are to one another.
- Subjects
AMINO acid sequence; HOMOLOGY (Biology); GLOBULINS; IMMUNOGLOBULINS; HLA histocompatibility antigens
- Publication
Scandinavian Journal of Immunology, 1978, Vol 8, Issue 6, p563
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1978.tb00557.x