Entrapment of proteins in phosphatidylcholine vesicles.
The trapping efficiency of globular proteins in four different types of phosphatidylcholine vesicles was systematically studied. Vesicles were generated in a mixture of 125I-labeled proteins of various molecular weights. The trapped proteins were separated from untrapped proteins by gel filtration and ultrafiltration and subsequently analyzed by gel electrophoresis and autoradiography. Entrapment of proteins was demonstrated by their resistance to trypsin digestion. The relative amount of each entrapped protein species was then compared to that of the original protein solution. In multilamellar vesicles and large unilamellar vesicles, proteins of molecular weight up to 97 000 had the same trapping efficiency as sucrose. In small unilamellar vesicles generated by either sonication or ethanol injection, however, the relative trapping efficiency of protein decreased progressively as the molecular weight of the protein became greater. For example, the trapping efficiency of alpha-amylase (Mr 97 000) was only half of that for sucrose. The apparent decrease in trapping efficiency with the protein's molecular weight in small unilamellar vesicles canbe accounted for by the combination of the bound water layer at the vesicle's internal surface and the steric hindrance when protein is captured during vesicle formation.
D002919:Chymotrypsinogen; D003207:Conalbumin; D007457:Iodine Radioisotopes; D008081:Liposomes; D008970:Molecular Weight; D009113:Muramidase; D010544:Peroxidases; D010713:Phosphatidylcholines; D011485:Protein Binding; D011506:Proteins; D000516:alpha-Amylases
D007457:Iodine Radioisotopes; D008081:Liposomes; D010713:Phosphatidylcholines; D011506:Proteins; D003207:Conalbumin; D002919:Chymotrypsinogen; D010544:Peroxidases; D000516:alpha-Amylases; D009113:Muramidase