agglutinative and hemolytic properties. We used affinity chromatograph, SDS-PAGE, far-western-blotting, MALDI-TOF/MS, and bioinformatics to determine the target of hemocyanin binding. Hemocyanin bound specifically to an ~The protein shared high homology withhrimp hemocyanin bound to human thioredoxin peroxide following the “lock - key model” at the tertiary structure level. Together, our data suggest that thioredoxin peroxide mediates, at least in part, the interaction between erythrocytes and shrimp hemocyaninagglutination and hemolysis