INHIBITION OF FRUIT BROMELAIN BY ITS UNIVALENT ANTIBODIES CROSS-REACTING AND NOT CROSS-REACTING WITH STEM BROMELAIN

概要

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Two anti-fruit bromelain antibody populations, cross-reacting and not cross-reacting with stem bromelain, were purified through ammonium sulfate precipitation, DEAE cellulose column chromatography and immunoaffinity chromatographies on immobilized stem and fruit bromelain columns. The univalent Fab antibodies were prepared from the above antibody populations (bivalent IgG antibodies) by papain digestion. Inhibition capacities of cross-reacting and noncross-reacting univalent antibodies on the caseinolytic (as a large nolecular weight substrate) or esterolytic (as a small molecular weight substrate) activities of fruit bromelain were compared with those of bivalent antibodies. The cross-reacting univalent antibody exhibited 100% inhibition of caseinolytic activity and 50% inhibition of esterolytic activity at the antibody excess region, whereas the noncross-reacting univalent antibody exhibited only 50% inhibition of caseinolytic activity and no inhibition of esterolytic activity. Kinetic analysis of the inhibitory action of the cross-reacting univalent antibody revealed that the inhibition was a noncompetitive type and the Ki value was 1.19×10^<-5> M from Dixon plots. These results were consistent with our previous concept that the active site of stem and fruit bromelain are involved in the structural homology between the two enzyme.
名古屋市立大学の論文
1983-07-25