Aromatic residues in the C-terminal helix of human apoC-I mediate phospholipid interactions and particle morphology[S]

Aromatic residues in the C-terminal helix of human apoC-I mediate phospholipid interactions and particle morphology[S]

Human apolipoprotein C-I (apoC-I) is an exchangeable apolipoprotein that binds to lipoprotein particles in vivo. In this study, we employed a LC-MS/MS assay to demonstrate that residues 38–51 of apoC-I are significantly protected from proteolysis in the presence of 1,2-dimyristoyl-3-sn-glycero-phosp...

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Bibliographic Details
Main Authors: Patrick F. James, Con Dogovski, Renwick C.J. Dobson, Michael F. Bailey, Kenneth N. Goldie, John A. Karas, Denis B. Scanlon, Richard A.J. O’Hair, Matthew A. Perugini
Format: Article
Language:English
Published: Elsevier 2009-07-01
Series:Journal of Lipid Research
Subjects:
analytical ultracentrifugation
apo
C1
CI
electron microscopy
lipid metabolism
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520307860

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http://www.sciencedirect.com/science/article/pii/S0022227520307860

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