Isolation and characterization of antigen-Ia complexes involved in T cell recognition
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Standard
Isolation and characterization of antigen-Ia complexes involved in T cell recognition. / Buus, S; Sette, A; Colon, S M; Jenis, D M; Grey, H M.
I: Cell, Bind 47, Nr. 6, 1986, s. 1071-7.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Isolation and characterization of antigen-Ia complexes involved in T cell recognition
AU - Buus, S
AU - Sette, A
AU - Colon, S M
AU - Jenis, D M
AU - Grey, H M
N1 - Keywords: Antigens; Chromatography, Gel; Histocompatibility Antigens; Histocompatibility Antigens Class II; Hybridomas; Hydrogen-Ion Concentration; Kinetics; Ovalbumin; T-Lymphocytes
PY - 1986
Y1 - 1986
N2 - Using equilibrium dialysis, it has been previously demonstrated that immunogenic peptides bind specifically to the Ia molecules serving as restriction elements in the immune response to these antigens. Using gel filtration to study the formation of ovalbumin (OVA) peptide-I-Ad complexes, it is herein demonstrated that the complexes, once formed, are very stable (kd approximately equal to 3 X 10(-6) s-1), but the rate of complex formation is very slow (ka approximately 1 M-1 s-1 explaining the overall low equilibrium constant of approximately 2 X 10(-6) M. Treating the complexes with glutaraldehyde revealed that the ovalbumin peptide was cross-linked solely to the alpha chain of I-Ad. Planar membranes containing I-Ad-OVA complexes stimulated a T cell response with 2 X 10(4) less antigen than required when uncomplexed antigen was used, thus demonstrating the biologic importance of these complexes in antigen recognition.
AB - Using equilibrium dialysis, it has been previously demonstrated that immunogenic peptides bind specifically to the Ia molecules serving as restriction elements in the immune response to these antigens. Using gel filtration to study the formation of ovalbumin (OVA) peptide-I-Ad complexes, it is herein demonstrated that the complexes, once formed, are very stable (kd approximately equal to 3 X 10(-6) s-1), but the rate of complex formation is very slow (ka approximately 1 M-1 s-1 explaining the overall low equilibrium constant of approximately 2 X 10(-6) M. Treating the complexes with glutaraldehyde revealed that the ovalbumin peptide was cross-linked solely to the alpha chain of I-Ad. Planar membranes containing I-Ad-OVA complexes stimulated a T cell response with 2 X 10(4) less antigen than required when uncomplexed antigen was used, thus demonstrating the biologic importance of these complexes in antigen recognition.
M3 - Journal article
C2 - 3490919
VL - 47
SP - 1071
EP - 1077
JO - Cell
JF - Cell
SN - 0092-8674
IS - 6
ER -
ID: 9947991