作者: V.P. Torchilin , V.G. Omel'Yanenko , A.L. Klibanov , A.I. Mikhailov , V.I. Gol'Danskii
DOI: 10.1016/0005-2736(80)90330-2
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摘要: The hydrophilic protein-enzyme, alpha-chymotrypsin, can be bound to the liposomal membrane after preliminary increase in hydrophobicity induced by acylation of protein amino groups with palmitic chloroanhydride. efficacy binding depends on degree modification. enzyme almost completely preserves its catalytic properties and ability interact a high molecular weight inhibitor. Binding performed during both process liposome formation incubation modified preformed liposomes. According ESR fluorescence spectroscopy, hydrophobic tail is incorporated into globule located surface membrane. Protein incorportation causes an amorphous nature membrane, not as mobile free protein. approach discussed useful soluble proteins artificial membranes.