Isolation and characterization of antigen-Ia complexes involved in T cell recognition

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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.

In: Cell, Vol. 47, No. 6, 1986, p. 1071-7.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Buus, S, Sette, A, Colon, SM, Jenis, DM & Grey, HM 1986, 'Isolation and characterization of antigen-Ia complexes involved in T cell recognition', Cell, vol. 47, no. 6, pp. 1071-7.

APA

Buus, S., Sette, A., Colon, S. M., Jenis, D. M., & Grey, H. M. (1986). Isolation and characterization of antigen-Ia complexes involved in T cell recognition. Cell, 47(6), 1071-7.

Vancouver

Buus S, Sette A, Colon SM, Jenis DM, Grey HM. Isolation and characterization of antigen-Ia complexes involved in T cell recognition. Cell. 1986;47(6):1071-7.

Author

Buus, S ; Sette, A ; Colon, S M ; Jenis, D M ; Grey, H M. / Isolation and characterization of antigen-Ia complexes involved in T cell recognition. In: Cell. 1986 ; Vol. 47, No. 6. pp. 1071-7.

Bibtex

@article{9fe79e90ebce11ddbf70000ea68e967b,
title = "Isolation and characterization of antigen-Ia complexes involved in T cell recognition",
abstract = "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.",
author = "S Buus and A Sette and Colon, {S M} and Jenis, {D M} and Grey, {H M}",
note = "Keywords: Antigens; Chromatography, Gel; Histocompatibility Antigens; Histocompatibility Antigens Class II; Hybridomas; Hydrogen-Ion Concentration; Kinetics; Ovalbumin; T-Lymphocytes",
year = "1986",
language = "English",
volume = "47",
pages = "1071--7",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "6",

}

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