A comparison of the surface activities of rat plasma apolipoproteins C-II, C-III-0, C-III-3.

@article{Krebs1983ACO,
  title={A comparison of the surface activities of rat plasma apolipoproteins C-II, C-III-0, C-III-3.},
  author={Keith E. Krebs and Michael C. Phillips and Charles E. Sparks},
  journal={Biochimica et biophysica acta},
  year={1983},
  volume={751 3},
  pages={
          470-3
        }
}

Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface.

It is concluded that apolipoproteins A-IV and B-17 display a combination of interfacial activity and elasticity particularly suited to stabilizing the surface of expanding triglyceride-rich particles.

A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II*

The results suggest that apoC-II regulates the activity of LPL in a pressure-dependent manner and is provided as a component of triacylglycerol-rich lipoproteins and is the co-factor for LPL as pressure increases.

Specificity of the lipid-binding domain of apoC-II for the substrates and products of lipolysis.

The difference in the extent of protein adsorption to lipid classes suggests that the distribution of apoC-II among lipoproteins will depend on their lipid composition and surface pressure.

Apolipoprotein C-I binds more strongly to phospholipid/triolein/water than triolein/water interfaces: a possible model for inhibiting cholesterol ester transfer protein activity and triacylglycerol-rich lipoprotein uptake.

To understand apoC-I's behavior at hydrophobic lipoprotein surfaces, oil drop tensiometry was used to compare the binding to triolein/water (TO/W) and palmitoyloleoylphosphatidylcholine/triolein/.

Structure and Interfacial Properties of Human Apolipoprotein A-V*

Spectroscopic and surface chemistry techniques revealed that apoA-V displays high affinity, low elasticity, and slow binding kinetics at hydrophobic interfaces, properties the authors propose may retard triglyceride-rich particle assembly.

Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic α-helices[S]

This model suggests that apolipoproteins have at least two interfacial conformations that are in a surface concentration and Π-dependent equilibrium, and provides insights into the selective metabolism and clearance of plasma lipoproteins and the process of lipoprotein remodeling.

The Interfacial Properties of ApoA-I and an Amphipathic α-Helix Consensus Peptide of Exchangeable Apolipoproteins at the Triolein/Water Interface*

Flexibility and surface pressure-mediated desorption and re-adsorption of apoA-I probably provides lipoprotein stability during metabolic-remodeling reactions in plasma.

Influence of the structure of the lipid-water interface on the activity of hepatic lipase.

Factors affecting the hydrolytic activity of purified rat hepatic lipase have been examined in mixed-monolayer systems and phase diagrams indicate transitions that suggest that triolein is forced out of the monolayer.

References

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Very low density lipoprotein. Removal of Apolipoproteins C-II and C-III-1 during lipolysis in vitro.

The results suggest that there is no preferential removal of apo-C-II or apolipoprotein C-III-1 from lipolyzed VLDL particles, and indicate that the ratio of Apo- c-II to c-III does not regulate the extent of lipolysis of different VLDl particles, at least in V LDL isolated from normolipidemic humans.

PROPERTIES OF APOLIPOPROTEINS AT THE AIR‐WATER INTERFACE *

The surface properties of rat apolipoprotein A-I (apoA-I), rabbit apoE, and bovine serum albumin (BSA) are compared so that the adsorption and surface denaturation of this globular protein make convenient points of reference and contrast for the apoprotein results.

Characterization of the rat apolipoproteins. I. The low molecular weight proteins of rat plasma high density lipoproteins.

Five low molecular weight proteins were purified from the last Sephadex fraction by ion exchange chromatography and all five proteins have apparent homologues among the human apolipoproteins.

Analysis of rat serum apolipoproteins by isoelectric focusing. I. Studies on the middle molecular weight subunits.

Analytical isoelectric focusing (IEF) has been applied to the study of the apolipoprotein components of rat serum high density and very low density lipoproteins and tends to rule out carbamylation or incomplete unfolding of the proteins in the presence of urea as the causes of the observed heterogeneity.

Lipid-protein interactions in the plasma lipoproteins.

Hepatic secretion of lipoproteins in the rat and the effect of experimental nephrosis.

It is postulated that the primary stimulus to hepatic plasma protein synthesis in response to proteinuria is general and that subsequent negative feedback regulation affects individual apolipoprotein synthesis rates, and that the biosynthesis and secretion of an apoprotein may be regulated independently of the lipoprotein density class in which it is found.