ISOLATION OF HEME-BINDING PROTEINS FROM VIBRIO-ANGUILLARUM USING AFFINITY-CHROMATOGRAPHY

Using affinity chromatography techniques, several hemin- and hemoglobi n-binding proteins of 97, 56 and 39 kDa were isolated from cell envelo pes of Vibrio anguillarum strain H775-3 (serotype O1) and of 56, 46 an d 37 kDa from strain RV22 (serotype O2). All these proteins were isola ted under iron-rich as well as iron-poor conditions. Proteins of 39 kD a in H775-3 and of 37 kDa in RV22 isolated by hemin affinity could als o bind biotinylated hemoglobin after being transferred to nitrocellulo se, which suggests that they could be the common receptors for the hem e group in V. anguillarum.