title: Alpha-haemolysin from E. coli. Purification and self-aggregation properties.
abstract: An improved, straightforward purification procedure for E.coli alpha-haemolysin has been developed. The protein exists in the form of large aggregates, held together mainly by hydrophobic forces. In the presence of urea or other chaotropic agents, the size of the aggregates decreases, while the specific activity is increased.
authors.affiliation: Department of Biochemistry, University of the Basque Country, Bilbao, Spain.
authors.forename: H
authors.initials: H
authors.lastname: Ostolaza
authors.forename: B
authors.initials: B
authors.lastname: Bartolomé
authors.forename: J L
authors.initials: JL
authors.lastname: Serra
authors.forename: F
authors.initials: F
authors.lastname: de la Cruz
authors.forename: F M
authors.initials: FM
authors.lastname: Goñi
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D001427:Bacterial Toxins / Q000302:isolation & purification*; D001665:Binding Sites; D002845:Chromatography; D004926:Escherichia coli / Q000032:analysis*; D029968:Escherichia coli Proteins; D006460:Hemolysin Proteins; D012995:Solubility; D014508:Urea
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; D029968:Escherichia coli Proteins; D006460:Hemolysin Proteins; C036507:Hlya protein, E coli; D014508:Urea