Abstract
Murine Ia and human DR antigens were isolated and purified by immunoprecipitation and sodium dodecyl sulfate/polyacrylamide gel electrophoresis with allo- and xenoantisera, respectively. The I-A subregion antigen consists of two chains, designated Aα, and Aβ, with molecular weights of 35.000 and 26.000, respectively. The I-C subregion antigen likewise consists of two chains, designated Cα and Cβ, with molecular weights of 32.000 and 29.000, respectively. Under nonreducing conditions, the Cβ chain migrates appreciably more rapidly on sodium dodecyl sulfate/polyacrylamide gels than the reduced Cβ chain, reflecting the presence of an intra-chain disulfide bond. The human DR antigen is also a two-chain unit and contains DRα and DRβ components with molecular weights of 34.000 and 28.000, respectively. The DRβ chain migrates more rapidly before reduction than afterward, like the murine Cβ chain. The DRβ and Cβ chains are also strikingly homologous if a single amino acid shift is imposed on one of those chains. Thus, human DR antigens strongly resemble the murine I-C subregion antigens.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3953-3956 |
| Number of pages | 4 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 75 |
| Issue number | 8 |
| State | Published - 1978 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Genetics
- General
Cite this
Murine Ia and human DR antigens. Homology of amino-terminal sequences. / Allison, J. P.; Walker, L. E.; Russell, W. A.; Pellegrino, M. A.; Ferrone, S.; Reisfeld, R. A.; Frelinger, Jeffrey A; Silver, J.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 75, No. 8, 1978, p. 3953-3956.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Murine Ia and human DR antigens. Homology of amino-terminal sequences
AU - Allison, J. P.
AU - Walker, L. E.
AU - Russell, W. A.
AU - Pellegrino, M. A.
AU - Ferrone, S.
AU - Reisfeld, R. A.
AU - Frelinger, Jeffrey A
AU - Silver, J.
PY - 1978
Y1 - 1978
N2 - Murine Ia and human DR antigens were isolated and purified by immunoprecipitation and sodium dodecyl sulfate/polyacrylamide gel electrophoresis with allo- and xenoantisera, respectively. The I-A subregion antigen consists of two chains, designated Aα, and Aβ, with molecular weights of 35.000 and 26.000, respectively. The I-C subregion antigen likewise consists of two chains, designated Cα and Cβ, with molecular weights of 32.000 and 29.000, respectively. Under nonreducing conditions, the Cβ chain migrates appreciably more rapidly on sodium dodecyl sulfate/polyacrylamide gels than the reduced Cβ chain, reflecting the presence of an intra-chain disulfide bond. The human DR antigen is also a two-chain unit and contains DRα and DRβ components with molecular weights of 34.000 and 28.000, respectively. The DRβ chain migrates more rapidly before reduction than afterward, like the murine Cβ chain. The DRβ and Cβ chains are also strikingly homologous if a single amino acid shift is imposed on one of those chains. Thus, human DR antigens strongly resemble the murine I-C subregion antigens.
AB - Murine Ia and human DR antigens were isolated and purified by immunoprecipitation and sodium dodecyl sulfate/polyacrylamide gel electrophoresis with allo- and xenoantisera, respectively. The I-A subregion antigen consists of two chains, designated Aα, and Aβ, with molecular weights of 35.000 and 26.000, respectively. The I-C subregion antigen likewise consists of two chains, designated Cα and Cβ, with molecular weights of 32.000 and 29.000, respectively. Under nonreducing conditions, the Cβ chain migrates appreciably more rapidly on sodium dodecyl sulfate/polyacrylamide gels than the reduced Cβ chain, reflecting the presence of an intra-chain disulfide bond. The human DR antigen is also a two-chain unit and contains DRα and DRβ components with molecular weights of 34.000 and 28.000, respectively. The DRβ chain migrates more rapidly before reduction than afterward, like the murine Cβ chain. The DRβ and Cβ chains are also strikingly homologous if a single amino acid shift is imposed on one of those chains. Thus, human DR antigens strongly resemble the murine I-C subregion antigens.
UR - http://www.scopus.com/inward/record.url?scp=0018104765&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0018104765&partnerID=8YFLogxK
M3 - Article
C2 - 99745
AN - SCOPUS:0018104765
VL - 75
SP - 3953
EP - 3956
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 8
ER -