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Fusion of phospholipid vesicles induced by the ribosome inactivating protein saporin
Author(s) -
Liu Guohong,
Hao Qiang,
Zhang Yah,
Gao Gui,
Yan Ganglin,
Yao Qizhi,
Li Qingshan
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203311
Subject(s) - vesicle , chemistry , phospholipid , saporin , fusion , ionic strength , biophysics , chromatography , crystallography , biochemistry , organic chemistry , biology , in vitro , membrane , immunotoxin , cytotoxicity , aqueous solution , linguistics , philosophy
The single chain ribosome‐inactivating protein Saporin‐S6 (SO‐6) induces the fusion of acid phospholipid vesicles. The extent of fusion was measured by resonance energy transfer assay between the N‐(7‐nitro‐2‐1,3‐benzoxadiazol‐4‐yl)‐dimyristoylphosphatidyl lithanolamine (NBD‐PE)(donor) and N‐(lissamine rhodamine B sulphonyl)‐diacylphoshaidylethanolamine (Rh‐PE) (acceptor) incorporated in the vesicle. The saturated lipid/protein molar ratio is approx. 100:1. The time course of fusion of vesicles induced by the protein showed that the process was completed within 10 minutes, and the size of the particles in the medium was enlarged which conforms the occurrence of the fusion occuring. The fusion is temperature dependent and the liquid‐crystalline state lipid is more apt to fuse than the gel phase lipid. The effect of SO‐6 is also dependent on ionic strength and pH, high salt concentration and basic pH may abolish fusion, which suggests that both electrostatic and hydrophobic components may be involved in the process.