Abstract
Colipase which is a polypeptide present in pancreas and pancreatic juice reactivates lipase which has been inhibited by bile salts. A complex, lipase—colipase—bile salts forms and this enzyme complex has a pH optimum for triglyceride hydrolysis of between 6 and 7 as compared with 8 to 9 for lipase alone. The colipase molecule has an excess of acidic residues and five disulphide bridges which account for its pH and thermal stability (Borgström and Erlanson, 1973).
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References
Borgström, B. and Erlanson, C. (1973). Pancreatic lipase and colipase. Interactions and effects of bile salts and other detergents. Europ. J. Biochem., 37, 60
Doyle, R. J., Bello, J. and Roholt, O. A. (1968). Probable protein crosslinking with tetranitromethane. Biochim. Biophys. Acta, 160, 274
Dufour, C, Sémériva, M. and Desnuelle, P. (1973). The role of carboxyl groups in the activity of pancreatic lipase. Biochim. Biophys. Acta, 327, 101
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Barrowman, J.A., Erlanson, C., Borgström, B. (1976). Effect of Chemical Modifications on the Function of Colipase. In: Rommel, K., Goebell, H., Böhmer, R. (eds) Lipid Absorption: Biochemical and Clinical Aspects. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-7176-2_15
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DOI: https://doi.org/10.1007/978-94-011-7176-2_15
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-011-7178-6
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