Immobilization of protein molecules on liposomes. Anchorage by artificially bound unsaturated hydrocarbon tails.
A method for the immobilization of trypsin, a hydrophilic nonmembrane protein, on a liposomal surface has been developed. The technique consists of covalent coupling of linoleoyl residues to the protein globules and consequent binding of linoleoyl trypsin to liposomes by a detergent dilution method. The immobilized protein preserved its biological functions: specific esterolytic catalytic activity and ability to bind to a macromolecular trypsin protein inhibitor. Liposomes carrying immobilized trypsin were able to sequester glucose with the same efficiency as liposomes without trypsin.
D007611:Aprotinin / Q000378:metabolism; D001665:Binding Sites / Q000187:drug effects; D055598:Chemical Phenomena; D002621:Chemistry; D004800:Enzymes, Immobilized / Q000378:metabolism*; D019787:Linoleic Acid; D008041:Linoleic Acids / Q000494:pharmacology; D008081:Liposomes; D010168:Palmitates / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism*
D004800:Enzymes, Immobilized; D008041:Linoleic Acids; D008081:Liposomes; D010168:Palmitates; C032023:palmitoyl chloride; D007611:Aprotinin; D019787:Linoleic Acid; D014357:Trypsin