title: Immunochemical studies of pancreatic colipase-lipase interaction employing immobilized synthetic peptides.
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.
authors: Institut de Chimie Biologique, Faculté Saint-Charles, Marseille, France.
authors: N
authors: N
authors: Rugani
authors: L
authors: L
authors: de la Fournière
authors: R
authors: R
authors: Julien
authors: L
authors: L
authors: Sarda
authors: J
authors: J
authors: Rathelot
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D002846:Chromatography, Affinity; D003089:Colipases / Q000302:isolation & purification / Q000378:metabolism*; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D006736:Horses; D007700:Kinetics; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000276:immunology; D010179:Pancreas / Q000201:enzymology*; D013552:Swine
chemical_list: D000906:Antibodies; D003089:Colipases; D009842:Oligopeptides; D008049:Lipase