Interaction of the α-Helices of Apolipophorin III with the Phospholipid Acyl Chains in Discoidal Lipoprotein Particles:  A Fluorescence Quenching Study†

Biochemistry ◽  
2001 ◽  
Vol 40 (47) ◽  
pp. 14279-14290 ◽  
Author(s):  
J. L. Soulages ◽  
E. L. Arrese
Keyword(s):  
Fluorescence Quenching ◽  
Lipoprotein Particles ◽  
Apolipophorin Iii ◽  
Acyl Chains ◽  
Phospholipid Acyl Chains

scholarly journals The phospholipid-dependence of uridine diphosphate glucuronyltransferase. Temperature-dependence of microsomal enzyme activity and thermotropic changes in membrane structure

1978 ◽  
Vol 175 (1) ◽  
pp. 115-124 ◽  
Author(s):  
D T Pechey ◽  
A B Graham ◽  
G C Wood
Keyword(s):  
Guinea Pig ◽  
Phospholipid Bilayer ◽  
Permeability Barrier ◽  
Uridine Diphosphate ◽  
Membrane Bilayer ◽  
Arrhenius Plots ◽  
Acceptor Activity ◽  
Microsomal Membranes ◽  
Acyl Chains ◽  
Phospholipid Acyl Chains

Arrhenius plots of the non-latent UDP-glucuronyltransferase (p-nitrophenol acceptor) activity of guinea-pig microsomal membranes prepared with 154 mM-KCl were linear from 5 to 40 degrees C. Arrhenius plots for other microsomal preparations from guinea pig and rat liver that show various degrees of transferase latency, exhibited two linear regions intersecting at a sharp transition point near 20-25 degrees C. This discontinuity was abolished or greatly decreased when transferase latency was removed by treating the membranes with perturbants of phospholipid bilayer strucutre. The fluorescent probe N-phenyl-1-naphthyl-amine detected a thermotropic change in the fluidity of the phospholipid acyl chains of all the microsomal membrane preparations studied, at temperatures close to those of the Arrhenius-plot transitions. It is concluded that the thermotropic change in the structure of the membrane bilayer probably is a ‘phase separation’ or clustering of phospholipids, which affects a permeability barrier that restricts access of substrate to the transferase molecules.

Influence of the sterol aliphatic side chain on membrane properties: a molecular dynamics study

2015 ◽  
Vol 17 (35) ◽  
pp. 22736-22748 ◽  
Author(s):  
João R. Robalo ◽  
J. P. Prates Ramalho ◽  
Daniel Huster ◽  
Luís M. S. Loura
Keyword(s):  
Molecular Dynamics ◽  
Membrane Properties ◽  
Side Chain ◽  
Side Chains ◽  
Aliphatic Side Chain ◽  
Acyl Chains ◽  
Hydrophobic Matching ◽  
Phospholipid Acyl Chains

Cholesterol provides best hydrophobic matching, induces maximal membrane ordering, and displays highest preference for saturated phospholipid acyl chains, among a homologous ser ies of sterols with side chains of varying lengths.

scholarly journals Vertical fluctuations of phospholipid acyl chains in bilayers

FEBS Letters ◽  
1987 ◽  
Vol 223 (1) ◽  
pp. 20-24 ◽  
Author(s):  
John R. Wardlaw ◽  
William H. Sawyer ◽  
Kenneth P. Ghiggino
Keyword(s):  
Acyl Chains ◽  
Phospholipid Acyl Chains

scholarly journals Role for phospholipid acyl chains and cholesterol in pulmonary infections and inflammation

2016 ◽  
Vol 100 (5) ◽  
pp. 985-997 ◽  
Author(s):  
Saame Raza Shaikh ◽  
Michael B. Fessler ◽  
Kymberly M. Gowdy
Keyword(s):  
Pulmonary Infections ◽  
Acyl Chains ◽  
Phospholipid Acyl Chains
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