The lung lamellar body as a functioning membrane in protein-catalyzed phosphatidylcholine transfer.
Lung lamellar bodies and liver mitochondria were used to demonstrate that soluble phospholipid transfer proteins from lung transfer phosphatidylcholine to both of these acceptors. The initial rate of transfer to lung lamellar bodies is about half that of the rate of transfer to the liver mitochondria when both acceptor membranes are present at saturating concentrations. Phosphatidylcholine unilamellar vesicles were used to demonstrate that the fatty acyl composition of the membrane phosphatidylcholine is a significant determinant of the rate of phosphatidylcholine transfer catalyzed by these proteins. The lamellar bodies have a unique phosphatidylcholine composition, and these studies suggest that this is an important factor in determining the lower initial rate of transfer to lamellar bodies. The studies have also characterized two phospholipid transfer proteins in rat lung in terms of isoelectric point. Isoelectric points for the two proteins which transfer phosphatidylcholine were found to be 5.6 +/- 0.08 and 6.2 +/- 0.03.
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002384:Catalysis; D004285:Dogs; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D008168:Lung / Q000378:metabolism* / Q000648:ultrastructure; D008563:Membrane Lipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000502:physiology*; D008930:Mitochondria, Liver / Q000378:metabolism; D010713:Phosphatidylcholines / Q000378:metabolism*; D051381:Rats
D002352:Carrier Proteins; D008563:Membrane Lipids; D008565:Membrane Proteins; D010713:Phosphatidylcholines