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α‐Haemolysin from E. coli purification and self‐aggregation properties
Author(s) -
Ostolaza Helena,
Bartolomé Borja,
Serra Juan L.,
de la Cruz Fernando,
Goñi Félix M.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80291-a
Subject(s) - chaotropic agent , chemistry , urea , hemolysin , escherichia coli , protein aggregation , chromatography , biophysics , biochemistry , biology , virulence , gene
An improved, straightforward purification procedure for E. coli α‐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.