Purification of the autotransporter protein Hbp of Escherichia coli.

S.J.M. van Dooren, J.R.H. Tame, S. Luirink, B. Oudega, B.R. Otto

Research output: Contribution to JournalArticleAcademicpeer-review


The enzyme Hbp (hemoglobin protease) of the pathogenic Escherichia coli strain EB1 has been purified to homogeneity by gel filtration chromatography. The purified protein is capable of binding heme and shows hemoglobin protease activity. Our method of purification is applicable not only to Hbp but also to other autotransporter proteins and will contribute to a better understanding of the function-structure relationship of this family of proteins. © 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
Original languageEnglish
Pages (from-to)147-150
Number of pages3
JournalFEMS Microbiology Letters
Publication statusPublished - 2001


Dive into the research topics of 'Purification of the autotransporter protein Hbp of Escherichia coli.'. Together they form a unique fingerprint.

Cite this