Isolation of heme-binding proteins from Vibrio anguillarum using affinity chromatography.
Using affinity chromatography techniques, several hemin- and hemoglobin-binding proteins of 97, 56 and 39 kDa were isolated from cell envelopes of Vibrio anguillarum strain H775-3 (serotype O1) and of 56, 46 and 37 kDa from strain RV22 (serotype O2). All these proteins were isolated under iron-rich as well as iron-poor conditions. Proteins of 39 kDa in H775-3 and of 37 kDa in RV22 isolated by hemin affinity could also bind biotinylated hemoglobin after being transferred to nitrocellulose, which suggests that they could be the common receptors for the heme group in V. anguillarum.
Mazoy
R
R
Departamento de Microbiología y Parasitología, Facultad de Ciencias, Universidad de Santiago de Compostela, Lugo, Spain.
Vázquez
F
F
Lemos
M L
ML
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D000081062:Heme-Binding Proteins; D006420:Hemeproteins / Q000737:chemistry / Q000302:isolation & purification*; D006427:Hemin; D008970:Molecular Weight; D014733:Vibrio / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D000081062:Heme-Binding Proteins; D006420:Hemeproteins; C017206:hemoglobin-binding protein, bacteria; D006427:Hemin