Detection and removal of an artefact fatty acid from the binding site of recombinant Bombyx mori pheromone-binding protein.
Recombinant Bombyx mori pheromone-binding protein (PBP), purified from an Escherichia coli expression system, has been found to contain (11Z)-octadecenoic acid (cis-vaccenic acid) as an artefact ligand. An efficient delipidation procedure is described to overcome what would appear to be a general problem with recombinant lepidopteran PBPs.
Oldham
N J
NJ
Max-Planck-Institute for Chemical Ecology, Carl-Zeiss-Promenade 10, D-07745 Jena, Germany. oldham@ice.mpg.de
Krieger
J
J
Breer
H
H
Svatos
A
A
D000818:Animals; D001665:Binding Sites / Q000502:physiology; D012831:Bombyx / Q000737:chemistry* / Q000502:physiology; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D019476:Insect Proteins / Q000737:chemistry; D036341:Intercellular Signaling Peptides and Proteins; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D013229:Stearic Acids / Q000737:chemistry*
C114874:5-octadecenoic acid; D002352:Carrier Proteins; D019476:Insect Proteins; D036341:Intercellular Signaling Peptides and Proteins; D011994:Recombinant Proteins; D013229:Stearic Acids; C403094:pheromone-binding protein, Bombyx