PMID:2579061: Difference between revisions

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<span style = 'font-size: large'> '''Suit, JL, Fan, ML, Kayalar, C and Luria, SE'''  (1985) Genetic study of the functional organization of the colicin E1 molecule.''J. Bacteriol.'' '''161''':944-8</span>
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!align=left  |Citation
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'''Suit, JL, Fan, ML, Kayalar, C and Luria, SE'''  (1985) Genetic study of the functional organization of the colicin E1 molecule. ''J. Bacteriol.'' '''161''':944-8
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!align=left  |Abstract
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2579061 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC214989 PMC214989]


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|{{TableHeadingColor}} |'''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.
!align=left  |Keywords
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Antibodies, Monoclonal/diagnostic use; Colicins/genetics; Colicins/immunology; Escherichia coli Proteins; Ion Channels; Liposomes; Receptors, Cell Surface; Receptors, Immunologic/metabolism; Structure-Activity Relationship
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2579061 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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==Annotations {{HelpIcon|Help:Literature}}==
==Annotations {{HelpIcon|Help:Literature}}==
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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Latest revision as of 04:44, 15 September 2013

Citation

Suit, JL, Fan, ML, Kayalar, C and Luria, SE (1985) Genetic study of the functional organization of the colicin E1 molecule. J. Bacteriol. 161:944-8

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.

Links

PubMed PMC214989

Keywords

Antibodies, Monoclonal/diagnostic use; Colicins/genetics; Colicins/immunology; Escherichia coli Proteins; Ion Channels; Liposomes; Receptors, Cell Surface; Receptors, Immunologic/metabolism; Structure-Activity Relationship

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