Abstract
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.
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