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  • Title: A quantitative assay to measure the interaction between immunogenic peptides and purified class I major histocompatibility complex molecules.
    Author: Olsen AC, Pedersen LO, Hansen AS, Nissen MH, Olsen M, Hansen PR, Holm A, Buus S.
    Journal: Eur J Immunol; 1994 Feb; 24(2):385-92. PubMed ID: 8299688.
    Abstract:
    A direct and sensitive biochemical assay to measure the interaction in solution between peptides and affinity-purified major histocompatibility complex (MHC) class I molecules has been generated. Specific binding reflecting the known class I restriction of cytotoxic T cell responses was obtained. Adding an excess of beta 2-microglobulin (beta 2m) significantly increased the rate of peptide association, but it did not affect the rate of dissociation. Binding was complicated by a rapid and apparently irreversible loss of functional MHC class I at 37 degrees C which might limit the life span of empty MHC class I thereby preventing the inadvertent exchange of peptides at the target cell surface. All class I molecules tested bound peptides of the canonical octa- to nona-meric length. However, one class I molecule, Kk, also bound peptides, which were much longer suggesting that the preference of class I molecules for short epitopes is not absolute and may be caused by factors other than the peptide-MHC class I binding event itself.
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