The effect of the cholesterol content in liposomes on their interaction with blood serum lipoproteins has been studied. It was shown that phosphatidyl choline liposomes without cholesterol did not interact selectively with any class of serum lipoproteins. At the same time, addition of high cholesterol concentrations to liposomes confers to them a new feature, namely the ability to interact selectively with the serum low density lipoproteins.
View Article and Find Full Text PDFBiochem Mol Biol Int
October 1993
The interaction of liposomes containing different amounts of cholesterol with human serum low density lipoproteins was investigated. Efficiency of the interaction depended on the cholesterol content of liposomes and was highest for liposomes with the maximal cholesterol/phospholipid molar ratio. The latter selectively and effectively interacted with low density lipoproteins, with up to 90% of lipoprotein particles interacting with liposomes in serum.
View Article and Find Full Text PDFThe interaction of liposomes containing different amounts of cholesterol with low-density lipoproteins from human serum was investigated. The efficiency of the interaction was found to depend on the cholesterol content of the liposomes and was highest for liposomes with the maximum cholesterol:phospholipid molar ratio. These liposomes selectively and effectively interacted with low-density lipoproteins; up to 90% of lipoprotein particles interacted with liposomes in serum.
View Article and Find Full Text PDFInteraction of lipid micelles (LM), containing cholesterol and hydroxycholesterol, with human serum lipoproteins was investigated. It was shown that cholesterol-containing LM interact with low density lipoproteins (LDL). Selectivity of LM-LDL interaction depended on the cholesterol content of micelles and almost did not depend on the composition of LM core.
View Article and Find Full Text PDFThe multiple forms of acid phosphatase from the hemolymph, fat body, intestinal wall and silk gland of the silkworm larvae differing in their mobility during polyacrylamide gel electrophoresis were separated by isoelectrofocusing, gel filtration and ion-exchange chromatography and characterized in terms of their molecular weight, isoelectric points and substrate specificity. It was found that silkworm tissues contain several enzyme forms possessing broad substrate specificity (EC 3.1.
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