Application of microcalorimetry to the study of lipid-protein interaction

Autor: F. Soetewey, Maryvonne Rosseneu, H. Peeters, Victor Blaton, J. Lievens
Rok vydání: 1976
Předmět:
Zdroj: Chemistry and Physics of Lipids. 17:38-56
ISSN: 0009-3084
DOI: 10.1016/0009-3084(76)90035-9
Popis: The enthalpy changes associated with protein-lipid binding were measured in an isothermal microcalorimeter. This technique was applied to the study of the association between albumin with fatty acid and lysolecithin, and between the plasma apolipoproteins and phospholipids. Microcalorimetry enables determination of the maximal enthalpy of binding and of complex stoichiometry in systems where one ligand, such fatty acid or a phospholipid is bound to either BSA or an apolipoprotein. The competition between 2 ligands, such as fatty acid and a dye for albumin can also be followed. The binding of synthetic phosphatidylcholines to the isolated major apoproteins of HDL and VLDL lipoprotein classes was compared by this technique. The maximal enthalpies decrease in the order apoA-II ⋍ apoC-III ∼ apoA-C > apoA-I , in agreement with the reported affinities of these peptides for phospholipids. Interapoprotein association between the two major apoproteins of apoHDL was demonstrated in the presence of phospholipids and compared to the behaviour of the whole apoHDL. Finally the association of two phosholipids naturally occurring in the HDL molecule was demonstrated. The interpretation and relevance of these various types of application of microcalorimetry to the study of protein-lipid systems is discussed and evaluated.
Databáze: OpenAIRE