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Serum of mud crab,  Scylla serrata  had antibacterial activity against certain host specific bacteria as well as other known crustacean pathogenic bacteria. The respective antibacterial molecule was isolated by ion-exchange chromatographic method using diethylaminoethyl-cellulose matrix and eluted with gradient increase of sodium chloride (0-0.5 M). There were three major peaks on the elution profile and fractions from second major peak exhibit differential antibacterial response against  Bacillus flexus  N3,  Escherichia coli ,  Vibrio harveyi  and  Vibrio vulnificus . The electrophoretic analyses of this fraction resulted in single protein band and the native molecular weight of this protein was found to be approximately 305 kDa. The bathocuproine sulfonic acid staining (a specific stain for copper), copper/protein ratio (0.129%) reveals this isolated antibacterial protein to be hemocyanin. This antibacterial hemocyanin is also capable of binding to cations, namely Ca 2+ , K + , Mg 2+ , Mn 2+  and Zn 2+  apart from carrying Fe 2+  ions. This native antibacterial hemocyanin was found to contain three or four subunits with possible molecular size of 70-98 kDa under reducing conditions. These findings indicate that the respiratory protein hemocyanin in the presence of cations functions as humoral immune molecule and the detailed investigation would reveal additional immune functional characteristics of this respiratory protein as well as subunits-specific functions of this antibacterial hemocyanin.

Cation metals specific hemocyanin exhibits differential antibacterial property in mud crab, Scylla serrata