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Hydrodynamic properties of phospho lipid vesicles and of sucrase iso maltase phospho lipid vesicles

, : Hydrodynamic properties of phospho lipid vesicles and of sucrase iso maltase phospho lipid vesicles. Journal of Biological Chemistry 256(17): 8977-8982

The hydrodynamic properties of phosphatidylcholine vesicles prepared by the cholate removal method were determined by analytical ultracentrifugation and compared with those of sonicated vesicles. The former were homogeneous as characterized by a narrow particle size distribution, but showed some fluctuation in the average particle size from one preparation to another. In contrast, sonicated vesicles showed a wide particle size distribution with their average particle diameter depending on the conditions of the ultrasonic irradiation. The molecular weight of the enzyme complex sucrase-isomaltase, which is a major intrinsic protein of [rabbit] small intestinal brush border membrane, was determined in the analytical ultracentrifuge in the presence of 2 different detergents: sodium cholate and octyl tetraoxyethylene. The values obtained were 2.7 .times. 105 and 2.8 .times. 105, respectively. Upon removal of the detergent, the protein aggregated to regular oligomeric structures which were spheroidal and had a diameter of 28 .+-. 4 nm (i.e., about twice the diameter of the sucrase-isomaltase complex). A model membrane system was reconstituted from phosphatidylcholine and sucrase-isomaltase by the cholate removal technique. Papain digestion of this model membrane yielded a water-soluble form of sucrase-isomaltase with a MW of 2.37 .+-. 0.09 .times. 105 indistinguishable from that obtained by papain digestion of brush border membrane vesicles. This finding supports the notion that the mode of lipid-protein interaction in the model membrane system resembles that in the brush border membrane. Reconstituted sucrase-isomaltase-phospholipid vesicles were investigated in the analytical ultracentrifuge. Depending on the protein/lipid ratio, populations with 1 to 6 protein molecules inserted into the lipid bilayer of 1 vesicle were observed. This shows unambiguously that the monomeric form of the protein is incorporated into the lipid bilayer. It was not possible to fit a Poisson distribution to the population of vesicles differing in the number of protein molecules inserted. This was attributed to the presence of some undissociated protein dimers which also interacted with the lipid bilayer.


PMID: 7263694

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