Affinity of serum apolipoproteins for lipid monolayers

Thesis/Dissertation · Thu Jan 01 04:00:00 EST 1987

OSTI ID:6155092

Ibdah, J A

The effects of lipid composition and packing as well as the structure of the protein on the affinities of apolipoproteins for lipid monolayers have been investigated. The adsorption of /sup 14/C-reductively methylated human apolipoproteins A-I and A-II at saturating subphase concentrations to monolayers prepared with synthetic lipids or lipoprotein surface lipids spread at various initial surface pressures has been studied. The adsorption of apolipoproteins is monitored by following the surface radioactivity using a gas flow counter and Wilhelmy plate, respectively. The physical states of the lipid monolayers are evaluated by measurement of the surface pressure-molecular area isotherms using a Langmuir-Adam surface balance. The probable helical regions in various apolipoproteins have been predicted using a secondary structure analysis computer program. The mean residue hydrophobicity and mean residue hydrophobic moment for the predicted helical segments have been calculated. The surface properties of synthetic peptides which are amphipathic helix analogs have been investigated at the air-water and lipid-water interfaces.

• Research Organization: Pennsylvania Univ., Philadelphia (USA)
• OSTI ID: 6155092
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ADSORPTION
AFFINITY
ANIMALS
APOLIPOPROTEINS
CARBON 14 COMPOUNDS
CHEMICAL COMPOSITION
COMPUTER CODES
CONFIGURATION
HELICAL CONFIGURATION
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
LIPIDS
LIPOPROTEINS
MAMMALS
MAN
MOLECULAR STRUCTURE
ORGANIC COMPOUNDS
PRIMATES
PROTEINS
SORPTION
TRACER TECHNIQUES
VERTEBRATES