Open AccessThe effect of the presence of integral membrane protein (human band 3) on the membrane lytic properties of melittin in reconstituted systems
Author(s) -
Veen Mark,
Cherry Richard J.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05897.x
Subject(s) - melittin , lysis , vesicle , phospholipid , band 3 , chemistry , membrane , biophysics , biochemistry , lytic cycle , lipid bilayer , salt (chemistry) , liposome , chromatography , membrane protein , biology , virus , virology
Reconstitution of the anion exchange protein from human erythrocytes (band 3) into phospholipid vesicles was shown to have a protective effect on melittin lysis of the vesicles when compared to pure lipid vesicles. Low salt buffer was found to cause an inhibition of lysis in both proteoliposomes and pure lipid vesicles compared to salt buffer. High phosphate concentration did not seem to cause inhibition of lysis in the reconstituted system. However, an inhibition is observed in pure lipid vesicle control, which is contradictory to previous reports.