linoleic-acid and palmitoyl-chloride

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.

Topics: Aprotinin; Binding Sites; Chemical Phenomena; Chemistry; Enzymes, Immobilized; Linoleic Acid; Linoleic Acids; Liposomes; Palmitates; Trypsin