Two-chain disulphide-bonded structure of antigen-specific T-helper factor: both chains are necessary for activity and their interaction is I-A restricted.
The molecular structure of the antigen-specific T-helper factor (ThF) which augments contact sensitivity in mice was studied. ThF was split into two types of polypeptide chain by mild reduction and alkylation; one antigen binding (which determined the specificity), the other non-antigen binding. The two chains were, by themselves, inactive but complemented each other and reconstituted biological activity. In addition, a genetic restriction was observed in the complementation of the two chains which mapped to the I-A subregion of the H-2 complex.
J A
JA
Little
G L
GL
Asherson
V
V
Colizzi
B M
BM
James
T
T
Hraba
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D003877:Dermatitis, Contact / Q000276:immunology; D004220:Disulfides; D000939:Epitopes / Q000276:immunology*; D005802:Genes, MHC Class II; D006183:H-2 Antigens / Q000235:genetics; D007375:Interleukin-1 / Q000032:analysis / Q000235:genetics / Q000276:immunology*; D051379:Mice; D008815:Mice, Inbred Strains
D004220:Disulfides; D000939:Epitopes; D006183:H-2 Antigens; D007375:Interleukin-1