Purification of the autotransporter protein Hbp of Escherichia coli.
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.
van Dooren
S J
SJ
Department of Molecular Microbiology, Institute of Molecular Biological Sciences, De Boelelaan 1087, 1081 HV Amsterdam, Netherlands.
Tame
J R
JR
Luirink
J
J
Oudega
B
B
Otto
B R
BR
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification; D017077:Culture Media, Conditioned / Q000737:chemistry; D010450:Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D006418:Heme / Q000378:metabolism; D008969:Molecular Sequence Data; D011817:Rabbits
D002352:Carrier Proteins; D017077:Culture Media, Conditioned; D006418:Heme; D010450:Endopeptidases; C114676:hemoglobin protease Hbp