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dc.contributor.authorWard, W.H.Jen
dc.date.accessioned2016-12-06T10:55:11Z
dc.date.available2016-12-06T10:55:11Z
dc.date.issued1982
dc.identifier.urihttp://hdl.handle.net/1842/18679
dc.description.abstractCholera "toxin binds to the outside of cells and one of its sub-units enters to activate adenylate cyclase. In the current work the nature of this action across the membrane was related to the hydrophobicities of cholera toxin and its subunits. Charge—shift electrophoresis showed that the proteins have no hydrophobic surfaces. Amino—acid composition and sequence data suggested that the molecules have no masked hydrophobic regions. Therefore part of cholera toxin may interact with polar molecules during its passage across the membrane.en
dc.publisherThe University of Edinburghen
dc.relation.ispartofAnnexe Thesis Digitisation Project 2016 Block 5en
dc.relation.isreferencedbyAlready catalogueden
dc.titleMechanism of action of cholera toxinen
dc.typeThesis or Dissertationen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnamePhD Doctor of Philosophyen


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