Interaction of apoA-II from human high density lipoprotein with lysolecithin.
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Interaction of apoA-II from human high density lipoprotein with lysolecithin.
The effects of lysolecithin and hexadecyltrimethylammonium bromide on the structure and stability of apoA-II from human high density lipoprotein have been evalued by circular dichroism and fluorescence measurements. There is a profound enhancement in the stability of apoA-II to guanidinium hydrochloride denaturation when it forms a phospholipid complex with lysolecithin micelles. This complex i...
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The binding of apoA-I to lysolecithin has been studied by fluorescence and circular dichroism. The influence of the conformation of apoA-I on its interaction with lysolecithin has also been evaluated. ApoA-I is bound to lysolecithin with an association greater than 10(7) whether apoA-I is native or highly unfolded in 1.8 M guanidinium hydrochloride. The association of apoA-I with lysolecithin r...
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There is in normal plasma an enzyme activity which converts labeled lysolecithin to lecithin by an energy-independent low density lipoprotein-activated pathway. Studies were undertaken to compare the identity of this enzyme with lecithin-cholesterol acyltransferase. During purification of the enzyme by ultracentrifugation and by chromatography on high density lipoprotein affinity column, DEAE-S...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)40306-1