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By R. J. P. Williams (auth.), Dr. Joe V. Bannister (eds.)

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HeUuo) into two bands, and the blood proteins of Cupiennius salei into three bands. Treatment with 50S and mercaptoethanol leads to the same pattern, in each of these species: A predominant band with a molecular weight of about 70,000 daltons, and two minor bands in equal proportion, which correspond to 95,000 and 110,000 daltons. The relation between the original pattern and the 50S-PAGE pattern is shown in Figure 1. Sedimentation studies, spectral analysis, and quantitative copper determinations have shown that the 70,000 dalton band represents the hemocyanin.

Experiments are under way to verify or to disprove this hypothesis. Turning now to a consideration of the oxygen binding properties of D. califoY'nica hemocyanin, we want to point out the marked sensitivity to pH changes, of both oxygen affinity and subunit cooperativity (Fig. 4). 0 pH Fig. 4. The change of oxygen affinity (uppeY'diagY'am) and cooperativity (loweY' diagY'am) with pH, in Dugesiella califoY'nica 37S hemocyanin. 1, 25 0 C, no Mg 2 +, no Ca 2 + 35 There is a strong positive Bohr effect and a fourfold change in nso within one pH unit.

Acad. Sci. : The structure of arthropod and mollusc hemocyanins. J. Bioi. Chern. 250, 3796-3806 (1975) Scorpion Hemocyanin Subunits: Properties, Dissociation, Association J. LAMY, J. -C. BAGLIN, AND J. , 1974) and oxygen binding studies (Padmanabhanaidu, 1966) have been reported. 5 ml per adult individual). This does not, however, lessen the choice of this animal in so much as one can miniaturize the study methods. In effect, its blood is at least 95% Hcy, and by an evolutional mystery, the subunits that constitute this molecule have so marked themselves during the ages that they have become easily separable, which does not seem to be the case with other arthropods.

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