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JBC, Vol. 250, Issue 18, 7300-7306, Sep, 1975

The interaction of apoA-I from human high density lipoprotein with lysolecithin

J. Gwynne, G. Palumbo, H. B. Brewer Jr and H. Edelhoch

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 results in an increase in secondary structure. A 25-residue fragment of apoA-I binds to lysolecithin equally strongly as the native molecule.
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