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Trypsin induced destabilization of liposomes composed of dioleoylphosphatidylethanolamine and glycophorin.

作者信息

Hu L R, Ho R J, Huang L

出版信息

Biochem Biophys Res Commun. 1986 Dec 30;141(3):973-8. doi: 10.1016/s0006-291x(86)80139-5.

DOI:10.1016/s0006-291x(86)80139-5
PMID:3814129
Abstract

Destabilization of liposomes composed of phosphatidylethanolamine (PE) and purified glycophorin of human erythrocytes was studied with the release of an entrapped fluorescent dye, calcein. Proteolytic cleavage of liposomes by trypsin induced a rapid increase of turbidity and the leakage of calcein from the liposomes. Kinetic experiments indicated that the destabilization was a second order reaction, i.e. it required liposome collision. Using N-(7-nitro-2,1,3-benzoxadiazol-4-yl) PE as a fluorescent probe for the formation of hexagonal phase of PE, tryptic digestion of the liposomes resulted in a higher tendency of the PE bilayer to transform into the hexagonal phase. We propose that hexagonal (or inverted micellar) structures are involved in the trypsin induced liposome destabilization.

摘要

相似文献

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2
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