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J. Biol. Chem., Vol. 276, Issue 21, 17796-17799, May 25, 2001

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SDS-induced Phenoloxidase Activity of Hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister^*

Heinz Decker^§, Margaret Ryan^¶, Elmar Jaenicke, and Nora Terwilliger

From the  Institute for Molecular Biophysics, University of Mainz, D55128 Mainz, Germany and ^¶ Oregon Institute of Marine Biology, University of Oregon, Charleston, Oregon 97420

Phenoloxidase, widely distributed among animals, plants, and fungi, is involved in many biologically essential functions including sclerotization and host defense. In chelicerates, the oxygen carrier hemocyanin seems to function as the phenoloxidase. Here, we show that hemocyanins from two ancient chelicerates, the horseshoe crab Limulus polyphemus and the tarantula Eurypelma californicum, exhibit O-diphenoloxidase activity induced by submicellar concentrations of SDS, a reagent frequently used to identify phenoloxidase activity. The enzymatic activity seems to be restricted to only a few of the heterogeneous subunits. These active subunit types share similar topological positions in the quaternary structures as linkers of the two tightly connected 2 × 6-mers. Because no other phenoloxidase activity was found in the hemolymph of these animals, their hemocyanins may act as a phenoloxidase and thus be involved in the primary immune response and sclerotization of the cuticle. In contrast, hemolymph of a more recent arthropod, the crab Cancer magister, contains both hemocyanin with weak phenoloxidase activity and another hemolymph protein with relatively strong phenoloxidase activity. The chelicerate hemocyanin subunits showing phenoloxidase activity may have evolved into a separate phenoloxidase in crustaceans.

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