STABILIZATION OF WHOLE MOLECULES OF GASTROPODAN HAEMOCYANINS BY CHLORHEXIDINE

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Abstract
Chlorhexidine diacetate 0.01% stabilized whole molecules of Helix pomatia .alpha.-hemocyanin under dissociating conditions; in 1 M NaCl and in 1.42 M sucrose. Dissociation at low ionic strength (10 mM) of the hemocyanin of Pila leopoldvillensis was also prevented by chlorhexidine. After dissociation into 1/2 molecules of H. pomatia .alpha.-hemocyanin in 1.42 M sucrose and of P. leopoldvillensis hemocyanin by lowering the ionic strength, whole molecules were formed on introduction by dialysis of chlorhexidine diacetate to a concentration of 0.01%. This stabilization points to the binding of the 2 chlorophenyl groups in hydrophobic regions of the protein and an ensuing crosslinking of the 1/2 molecules of gastropodan hemocyanins. Chlorguanide, which almost corresponds to 1/2 chlorhexidine, even at a concentration of 0.1%, only slightly stabilized the whole molecules.