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P Pontarotti

Publications and source records attributed to P Pontarotti.

57 records · Page 4Linked to original sources

Cross-reactivity of a monoclonal anti-[Met5]enkephalin antibody with cholecystokinin peptides.

The hypothesis of a conformational similarity between the unsulfated form of cholecystokinin C-terminal heptapeptide and [Met5]enkephalin was proposed by Schiller and colleagues. To test this possibility, we investigated the competition of cholecystokinin C-terminal peptides for the binding to a monoclonal anti-[Met5]enkephalin antibody. We observed that the antibody immunoprecipitated cholecystokinin peptides having at least the six C-terminal amino acids. Unlike the opiate receptors which had no affinity for the sulfated heptapeptide, the monoclonal antibody recognized the sulfated form of the C-terminal octapeptide of cholecystokinin.

Amino Acid Sequence↗

Serological and structural analysis of HLA class I molecules: beta 2-microglobulin interacts with the two external domains of the HLA class I heavy chain.

The serological reactivities of HLA class I molecules were studied in relation to structural modifications of these molecules, including shuffling of external exons and exchange of human beta 2-microglobulin for beta 2-microglobulin from different species. Two major clusters (I and II) of monomorphic and polymorphic antigenic determinants could be delineated. beta 2-Microglobulin participates in the formation of the two clusters, indicating that the light chain interacts tightly with the two external domains of the HLA class I heavy chain. However, external molecules can modify these interactions and alter the antigenic structure of the overall molecule. Thus, fixation on HLA class I molecules of the Fab fragment of a monoclonal antibody directed at antigenic determinants associated with cluster II resulted in enhanced fixation of a monoclonal antibody (B10.6) related to cluster I. The structural and functional implications of these results are discussed.

Antibodies, Monoclonal↗