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Hemocyanin (Hc) is a multifunctional protein in both mollusks and arthropods.   Phenoloxidase (PO) activities are the most important physiological functions   for Hcs after conversion. In shrimp, Hc occurs as two oligomer forms,   dodecamers and hexamers. Differences in the transport oxygen capacity and   agglutination activity between the two oligomers of shrimp Hc have been   found. In the present study, we investigated the differences in the   Hc-derived PO activity between the dodecameric and hexameric Hc forms of the   shrimp Litopenaeus vannamei. The two oligomers were separated by   non-denaturing polyacrylamide gel electrophoresis, converted by trypsin   cleavage and their PO activities were determined by oxidation of L-DOPA. The   dodecamers exhibited PO activity after enzymatic conversion while the   hexamers did not exhibit PO activity. This result provides new insight into   the structural/functional relationships of Hcs

Hemocyanin-derived phenoloxidase activity is dependent on dodecameric structure in shrimp Litopenaeus vannamei