Tachypleus tridentatus Hemocyanin

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Abstract
Hemocyanin monomers were isolated from Tachypleus tridentatus hemolymph by gel chromatography on Sephadex G-100. The isolated monomers were separated into four fractions by DEAE-Sephadex chromatography; they comprised 6 different subunits, designated as αζ-C chains. All of them showed the same molecular weight, 70, 000, on SDS-gel electrophoresis. The ζ chain was eluted ahead of the other subunits during gel chromatography. It tended to dimerize during prolonged dialysis or purification procedures. The γ and δ chains were isolated in pure form. The γ and ε chains, and also the β and ε chains, were obtained as mixtures but were not separated from each other. All the subunits showed different antigenicities. The amino-terminal portions of the a through a chains have the same sequence, Thr-Ile-Leu-Lys-Glu-Lys-GIn. The ζ chain has a different amino-terminal sequence, ValLeu-Asp-X-Ile/Leu-Glu-Lys. The ζ chain contained only 1 mol of Cu/mol of protein, whereas the other chains contained 2 mol of Cu/mol of protein. No free sulfhydryl group was detected in the absence of guanidine. However, 3 mol of SH/mol of protein was detected immediately after the addition of 6 m guanidine-HCI. These SH groups were very unstable and disappeared on standing.

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