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PANCREATIC LIPASE/COLIPASE BINDING SITE INVESTIGATION
Chaillan, Catherine Foglizzo, Edith Granon, Simone Lombardo, Dominique Chapus, Catherine
Chaillan, Catherine
Foglizzo, Edith
Granon, Simone
Lombardo, Dominique
Chapus, Catherine
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Issue Date
1991
Submitted date
2024-03-27
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Abstract
Pancreatic lipase is responsible for fat digestion in the intestine. The enzyme, which belongs to a special class of esterases, realizes an heterogeneous catalysis. In vivo, because of the strong inhibitory effect of bile salt,the lipase action requires the presence of a small pancreatic protein, colipase, the function of which is to anchor lipase to the bile salt coated lipid interface. The function of the lipase/colipase system requires the presence of two topographically distinct binding sites on both proteins, an interfacial binding site and a protein binding site. Up to now, only the colipase interfacial binding site is well documented. In order to locate the lipase/colipase binding site on each partner, a covalent cross-linked complex has been obtained using carbodiimides. Immunological analysis of the complex clearly confirms the presence of lipase and colipase. The complex has a Mr (60 kDa) consistent with a stoichiometry of one mol colipase per mol lipase and retains its catalytic efficiency towards emulsified substrates. Moreover, the use of carbodiimides to cross-link lipase and colipase unambiguously shows the participation of ion-pairing in the interaction between the two proteins.
Citation
Lipases : structure, mechanism and genetic engineering, 321 - 324
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Type
Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
EISSN
ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International