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

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...

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Bibliographic Details
Published in:The Journal of biological chemistry 1975-09, Vol.250 (18), p.7300-7306
Main Authors: J Gwynne, G Palumbo, H B Brewer, Jr, H Edelhoch
Format: Article
Language:English
Subjects:
Apoproteins - blood
Binding Sites
Circular Dichroism
Guanidines
Humans
Kinetics
Lipoproteins, HDL - blood
Lysophosphatidylcholines
Mathematics
Protein Binding
Protein Conformation
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Succinates
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)40944-7