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By Karl M. Wilbur, Peter W. Hochachka

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233-248. Academic Press, New York. , and Beltramini, M. (1979). The hemocyanin of Aplysia limacina: chemical and functional characterization. Comp. Biochem. Physiol. A 62A, 579-584. , and Zanotti, G. (1981). Structural studies on molluscan hemocyanins. In "Invertebrate Oxygen-Binding Proteins. Structure, Active Site, and Function" (J. Lamy and J. ), pp. 393-404. Dekker, New York. Ghisotti, F. (1976). Malacological discoveries in the Mediterranean: report of some exotic species. Conchiglie {Milan) 12, 269-272.

This chain has 1. Respiratory Pigments: Structure and Function 23 acetylvaline at its N-terminus and, with 153 residues, is the longest invertebrate globin chain thus far reported. Its sequence and alignment with a number of other globins are shown in Table IV. As can be seen, the extra length of the chain is due to an extension of the N-terminal end of the molecule. It is also of interest that only two histidyl residues, which correspond to the proximal and distal histidines that link the heme to the globin, are present.

Atlas of Protein Sequence and Structure," Vol. 5, Suppl. 1. Nat. Biomed. Res. C. Deaton, L. , and Mangum, C. P. (1976). The function of hemoglobin in the arcid clam Noetia ponder osa—II. Oxygen uptake and storage. Comp. Biochem. Physiol. A 53A, 181-186. DePhillips, H. , Nickerson, K. , and Van Holde, K. E. (1969). Physical studies of hemocyanins. IV. Oxygen-linked disassociation of Loligo pealei hemocyanin. Biochemistry 8, 3665-3672. DePhillips, H. , Nickerson, K. , and Van Holde, K. E. (1970).

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