title: Genetic study of the functional organization of the colicin E1 molecule.
abstract: Colicin E1 fragments obtained by genetic manipulations of the ColE1 plasmid were tested for bactericidal activity, binding to bacterial cells, and reactions with a series of anticolicin monoclonal antibodies. Two of the fragments were also tested for ability to form channels in liposomal vesicles. The results are in agreement with studies from chemically and enzymatically derived colicin fragments, assigning the receptor binding activity to the central part of the molecule and the killing activity to a region near the carboxyl terminus.
authors.forename: J L
authors.initials: JL
authors.lastname: Suit
authors.forename: M L
authors.initials: ML
authors.lastname: Fan
authors.forename: C
authors.initials: C
authors.lastname: Kayalar
authors.forename: S E
authors.initials: SE
authors.lastname: Luria
mesh_terms: D000911:Antibodies, Monoclonal; D003087:Colicins / Q000235:genetics / Q000276:immunology; D029968:Escherichia coli Proteins; D007473:Ion Channels; D008081:Liposomes; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D000911:Antibodies, Monoclonal; D003087:Colicins; D029968:Escherichia coli Proteins; D007473:Ion Channels; D008081:Liposomes; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; C028593:colicin receptor, E coli