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.

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@article{Ostolaza1991AlphahaemolysinFE, title={Alpha-haemolysin from E. coli. Purification and self-aggregation properties.}, author={Helena Ostolaza and Borja Bartolom{\'e} and J. Serra and Fernando de la Cruz and F{\'e}lix M Go{\~n}i}, journal={FEBS letters}, year={1991}, volume={280 2}, pages={195-8} }