Apolipoprotein A-II and structure of human serum high density lipoproteins

Journal Article · Tue Apr 10 04:00:00 EST 1979 · J. Biol. Chem.; (United States)

OSTI ID:5373743

Ritter, M C; Scanu, A M

The results indicate that (a) apo-A-II can generate HDL complexes, although these are heterogeneous in size and density; (b) the formation of these complexes requires well defined conditions, particularly with regard to initial protein concentration and lipid/protein ratio; (c) below and above the optimal apo-A-II concentration for HDL reassembly, reassociation of apo-A-II with lipids is minimal, probably due to changes in conformation or state of association, or both, of the apoprotein; and (d) at lipid/apo-A-II ratios above 1, the formation of lipid-rich particles is due to a process characterized by an adsorption of apo-A-II to thermodynamically stable lipid vesicles followed by their disruption into particles heterogeneous in size and density. We conclude that the interaction of apo-A-II with HDL lipids is extremely sensitive to experimental conditions and that apo-A-II can be incorporated into lipoprotein particles of much broader distribution than those previously obtained in similar reassembly studies involving apolipoprotein A-I.

• Research Organization: Univ. of Chicago, IL
• OSTI ID: 5373743
• Journal Information: J. Biol. Chem.; (United States), Journal Name: J. Biol. Chem.; (United States) Vol. 254:7; ISSN JBCHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
APOLIPOPROTEINS
BIOCHEMICAL REACTION KINETICS
BIOCHEMISTRY
CHEMISTRY
COMPLEXES
DENSITY
IN VITRO
KINETICS
LIPIDS
LIPOPROTEINS
ORGANIC COMPOUNDS
PH VALUE
PHYSICAL PROPERTIES
PROTEINS
QUANTITY RATIO
REACTION KINETICS
STOICHIOMETRY
STRUCTURAL CHEMICAL ANALYSIS