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Interactions of bile salt micelles and colipase studied through intermolecular nOes
Author(s) -
Dominguez Cyril,
Sebban-Kreuzer Corinne,
Bornet Olivier,
Kerfelec Brigitte,
Chapus Catherine,
Guerlesquin Françoise
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02034-2
Subject(s) - colipase , micelle , chemistry , nuclear magnetic resonance spectroscopy , nuclear overhauser effect , lipase , biochemistry , stereochemistry , pancreatic lipase , organic chemistry , enzyme , aqueous solution
Colipase is a small protein (10 kDa), which acts as a protein cofactor for the pancreatic lipase. Various models of the activated ternary complex (lipase–colipase–bile salt micelles) have been proposed using detergent micelles, but no structural information has been established with bile salt micelles. We have investigated the organization of sodium taurodeoxycholate (NaTDC) micelles and their interactions with pig and horse colipases by homonuclear nuclear magnetic resonance (NMR) spectroscopy. The NMR data supply evidence that the folding of horse colipase is similar to that already described for pig colipase. Intermolecular nuclear Overhauser effects have shown that two conserved aromatic residues interact with NaTDC micelles.