The enzyme Hbp (hemoglobin protease) of the pathogenic Escherichia coli str
ain EB1 has been purified to homogeneity by gel filtration chromatography.
The purified protein is capable of binding heme and shows hemoglobin protea
se activity. Our method of purification is applicable not only to Hbp but a
lso to other autotransporter proteins and will contribute to a better under
standing of the function-structure relationship of this family of proteins.
(C) 2001 Federation of European Microbiological Societies. Published by El
sevier Science B.V. All rights reserved.