Isolation and Lipid Binding Properties of the Low Molecular Weight Protein Components of Bovine High Density Lipoprotein

Gel filtration elutions of DMPC/bovine ApoC mixtures with these four proteins demonstrated that unilamellar vesicles also become disrupted. D(,2) and D(,3) were able to form a complex of essentially the same size and stoichiometry under a variety of initial lipid: protein ratios. Recombinants with D(,4) were less discrete, with the size and stoichiometry of complexes being dependent on the initial lipid: protein ratio used. The complexes formed are of a size (2 to 3 x 10('5) daltons) and weight percentage protein composition (30-40%) comparable to intact bovine HDL. Isopycnic density gradient ultracentrifugational isolations of complexes demonstrated that DMPC/bovine ApoC recombinants routinely banded within the density range of intact bovine HDL, 1.063 - 1.125 g/ml.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• Patterson, Bruce Wayne

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(UMI)AAI8018198

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/67397