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Proteolytic cleavage of the bacterial protein toxin pneumolysin with protease K creates two fragments of 37 and 15 kDa. This paper describes the purification of these two fragments and their subsequent physical and biological characterisation. The larger fragment is directly involved in the cytolytic mechanism of this pore-forming protein, via membrane binding and self-association. The smaller fragment lacks ordered structure or discernible activity.

Original publication

DOI

10.1016/s0014-5793(97)00838-7

Type

Journal article

Journal

FEBS letters

Publication Date

08/1997

Volume

412

Pages

563 - 567

Addresses

Department of Microbiology and Immunology, University of Leicester, UK.

Keywords

Hemolysis, Endopeptidase K, Peptide Fragments, Bacterial Proteins, Streptolysins, Liposomes, Spectrometry, Fluorescence, Circular Dichroism, Protein Binding, Structure-Activity Relationship, Hydrolysis