Acid-base titration of hemocyanin from Octopus vulgaris

Photochemical effects associated with the copper absorption bands of the native hemocyanin from Octopus vulgaris

“…Therefore, the calculated number of modified histidines (6 residues per 2 Cu atoms) represents a minimum number of ligands for the metal ions. These results are in agreement with the data obtained by acidbase titration of hemocyanin [9].…”

The Binding of 1‐Anilino‐8‐naphthalene Sulfonate to the Hemocyanin of Octopus vulgaris

“…It is unlikely, therefore, that the removal of the metal induces the appearence of a new binding site for such a large molecule as ansyl. Finally, potentiometric titrations of hemocyanin [26], as well as Raman spectroscopic studies [33], have demonstrated the highly hydrophobic character of the metal binding site; our results indicate that the binding site of ansyl is equally hydrophobic. Taken together, the data presently available suggest that the ansyl and copper binding sites are coincident.…”

“…Native and apo-hemocyanin from Octopus vulgaris have been prepared as described elsewhere [24,26]. The apoprotein contains 12-15% of the original copper.…”

“…In any case, the binding probably depends on hydrophobic interactions although ionic bonds involving the sulfonate group may be also important [26].…”

Copper transfer between Neurospora copper metallothionein and type 3 copper apoproteins

“…Fully oxygenated tyrosinase and hemocyanin showed absorption ratios ofAags/A28o = 0.1 7 [4] and A 3~7/A 278 = 0.18 [5], respectively. Apotyrosinase and apohemocyanin were prepared by KCN treatment according to [6] and [7], respectively. X-band EPR measurements were performed at 90 K using a Varian E-112 spectrometer.…”