Dissertation/Thesis Abstract

Acetylation of apolipoprotein A-I and its effect on lipopolysaccharide binding
by Adams, Christopher, M.S., California State University, Long Beach, 2012, 83; 1521609
Abstract (Summary)

Apolipoprotein A-I (apoA-I) is a major component of High Density Lipoproteins (HDL) and is comprised of 6 amphipathic α-helices in an N-terminal bundle and a smaller C-terminal region. Studies have suggested that HDL and apoA-I have the ability to neutralize the effects of lipopolysaccharides (LPS), the major cause of sepsis. ApoA-I was acetylated to neutralize the positive charge of the lysine residues prior to determining the effects on LPS binding. The acetylation procedure did not alter the stability of apoA-I though the α-helical content was reduced. Upon analysis by mass spectrometry it was determined that nearly 1000% of the lysine residues were neutralized. Using NativePAGE, Far-UV analysis, 1-anilinonaphthalene-8-sulfonate, and tryptophan fluorescence it was determined that when the positive lysine residues were neutralized, LPS binding was strongly impaired, indicating that lysine residues have a critical role in LPS binding.

Indexing (document details)
Advisor: Weers, Paul M. M.
Commitee: McAbee, Douglas D., Narayanaswami, Vasanthy, Weers, Paul M. M.
School: California State University, Long Beach
Department: Biochemistry
School Location: United States -- California
Source: MAI 51/04M(E), Masters Abstracts International
Source Type: DISSERTATION
Subjects: Biochemistry
Keywords:
Publication Number: 1521609
ISBN: 9781267790385
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