Interactions of Colipase with Bile Salt Micelles

• Published in: European journal of biochemistry Vol. 58; no. 2; pp. 555 - 559
• Main Authors: CHARLES, Maurice, ASTIER, Martine, SAUVE, Paul, DESNUELLE, Pierre
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01-10-1975
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1975.tb02405.x

A detailed investigation by ultracentrifugation of the colipase‐taurodeoxycholate system showed the formation of well‐defined mixed associations with a sedimentation coefficient of about 2.2 S. The fact that these associations were only detectable above the critical micelle concentration of the salt indicated that micelles rather than monomers were bound to the cofactor.
Two technical difficulties must be overcome before the weight of the associations could be measured with a reasonable accuracy. Firstly, the partial specific volume of the associations was determined using a digital microdensimeter and the interferometric system of the ultracentrifuge for concentration determinations. Secondly, due to the fact that micelle concentrations could not be equilibrated by dialysis, even after an extended period of time, an appropriate dilution of the ligand in the buffer compartment was necessary in order to compensate for its fixation by colipase in the solution. Then, the ionic strength dependence of the weight of the associations was found to vary in parallel with that of the micelles and to be in each case equal to the sum of the weights of one colipase molecule and one micelle. Therefore, colipase can be expected to contain a single high affinity site for bile salt micelle binding.