@article{9c139060ba2f11ddae57000ea68e967b,
title = "Establishment of a quantitative ELISA capable of determining peptide - MHC class I interaction.",
abstract = "Many different assays for measuring peptide-MHC interactions have been suggested over the years. Yet, there is no generally accepted standard method available. We have recently generated preoxidized recombinant MHC class I molecules (MHC-I) which can be purified to homogeneity under denaturing conditions (i.e., in the absence of any contaminating peptides). Such denatured MHC-I molecules are functional equivalents of {"}empty molecules{"}. When diluted into aqueous buffer containing beta-2 microglobulin (beta2m) and the appropriate peptide, they fold rapidly and efficiently in an entirely peptide dependent manner. Here, we exploit the availability of these molecules to generate a quantitative ELISA-based assay capable of measuring the affinity of the interaction between peptide and MHC-I. This assay is simple and sensitive, and one can easily envisage that the necessary reagents, standards and protocols could be made generally available to the scientific community.",
author = "C Sylvester-Hvid and N Kristensen and T Blicher and H Ferr{\'e} and Lauem{\o}ller, {S L} and Wolf, {X A} and K Lamberth and Nissen, {Mogens Holst} and Pedersen, {L {\O}} and S Buus",
note = "Keywords: Buffers; Enzyme-Linked Immunosorbent Assay; Histocompatibility Antigens Class I; Humans; Peptides; Protein Binding; Protein Renaturation; Sensitivity and Specificity; beta 2-Microglobulin",
year = "2002",
language = "English",
volume = "59",
pages = "251--8",
journal = "HLA",
issn = "2059-2302",
publisher = "Wiley",
number = "4",
}