Immunochemical studies of pancreatic colipase-lipase interaction employing immobilized synthetic peptides. |
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Authors: | N Rugani L de la Fournière R Julien L Sarda J Rathelot |
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Affiliation: | Institut de Chimie Biologique, Faculté Saint-Charles, Marseille, France. |
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Abstract: | In view to study the possible participation of the sequence portions of colipase including or close to the free carboxyl groups at positions 15 and/or 72 to the binding with pancreatic lipase, we have used three synthetic peptides matching portions 8-16, 59-67 and 67-72 of the amino acid sequence. Polyclonal rabbit anticolipase immune serum, which cross-reacts with peptides in ELISA, was fractionated on columns of peptide coupled to Sepharose. Of the three fractions of antibodies, only that interacting with peptide 8-16 had the capacity to inhibit colipase-dependent lipase activity by specifically preventing the association of lipase with its protein cofactor previously bound to lipid. We conclude that the region spanning residues 8-16 of colipase is of importance for colipase-lipase interaction in the active complex formed at interface. |
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