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J. Biol. Chem., Vol. 259, Issue 8, 4739-4749, 04, 1984

The structure of the hemocyanin from the horseshoe crab, Limulus polyphemus. The amino acid sequence of the largest cyanogen bromide fragment

E Yokota and AF Riggs

The amino acid sequence of the largest CNBr fragment, CNBrIa, from hemocyanin II of Limulus polyphemus has been determined. This fragment contains 203 residues, has Mr = 23,600, and is the NH2-terminal segment of the molecule. Comparison of this sequence with the first 87 residues of the NH2-terminal sequence of the alpha chain of hemocyanin from the Japanese horseshoe crab, Tachypleus tridentatus, of the Western Pacific (Nemoto, T., and Takagi, T. (1981) Biochim. Biophys. Acta 670, 79-83) shows that 46% of the residues are identical. Residues 172-177, -His- His-Trp-His-Trp-His-, appear to constitute at least part of the copper- binding site. This conclusion is supported by our finding that 40% of the residues in the sequence 172-186 are identical to residues 188-202 in tyrosinase from Neurospora; residues 188 and 193 in tyrosinase are known to be copper-binding histidines (Pfiffner, E., and Lerch, K. (1981) Biochemistry 20, 6029-6035). Model building suggests that histidines 172 and 175 might bind one copper atom and histidines 173 and 177 might bind the second copper. These observations suggest that tyrosinase and hemocyanin may have a common evolutionary origin, but we have not so far seen other correspondences.
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				B Linzen, N. Soeter, A. Riggs, H. Schneider, W Schartau, M. Moore, E Yokota, P. Behrens, H Nakashima, T Takagi, et al. The structure of arthropod hemocyanins Science, August 9, 1985; 229(4713): 519 - 524. [Abstract] [PDF]