PMID: 16910Jun 10, 1977

Interaction of apoA-II from human high density lipoprotein with lysolecithin

The Journal of Biological Chemistry
G Palumbo, H Edelhoch


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 is not only resistant to guanidinium hydrochloride denaturation, but it can be formed in a 6 M solution of this denaturant. The behavior of apoA-II in the native human high density protein is much closer to that of the lysolecithin apoA-II complex than to that of the free apoA-II.

Related Concepts

Circular Dichroism, Vibrational
Hydrogen-Ion Concentration
Alpha-1 Lipoprotein
Protein Conformation
Protein Denaturation
Fluorescence Spectroscopy

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