Interaction of amphiphilic substrates (acyl-CoAs) and their metabolites (free fatty acids) with microsomes from mouse sciatic nerves.
We have measured the partition of stearoyl-CoA and oleoyl-CoA between an aqueous phase and the microsomes from mouse sciatic nerves. A method of microultracentrifugation was used which allowed us to study separately the aqueous phase and the biological membranes. We observed that the partition is dependent upon the amount of acyl-CoAs and membrane proteins but seems to be independent of time. A theoretical analysis of these data allowed interpretation of the binding and release in terms of acyl-CoA surface density in the vesicles. We have also analyzed the fate of the membrane-bound acyl-CoAs. We show that, whereas the apparent partition does not seem to vary, the hydrolysis of the membrane-bound acyl-CoAs followed by the release of free fatty acids from the membrane leads to a modification of the partition of acyl-CoAs between the membrane and the aqueous phase. We propose that there is a constant partition of the aliphatic chains (acyl-CoAs + free fatty acids).
Juguelin
H
H
Institut de Biochimie Cellulaire et de Neurochimie du CNRS, Université de Bordeaux II, France.
Bessoule
J J
JJ
Cassagne
C
C
D000214:Acyl Coenzyme A / Q000378:metabolism* / Q000494:pharmacology; D000818:Animals; D003065:Coenzyme A / Q000494:pharmacology; D005230:Fatty Acids, Nonesterified / Q000378:metabolism*; D006358:Hot Temperature; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D008861:Microsomes / Q000378:metabolism*; D008956:Models, Chemical; D011485:Protein Binding; D012584:Sciatic Nerve / Q000378:metabolism*; D012710:Serum Albumin, Bovine; D012995:Solubility
D000214:Acyl Coenzyme A; D005230:Fatty Acids, Nonesterified; D008565:Membrane Proteins; D012710:Serum Albumin, Bovine; D003065:Coenzyme A