Beltramini M, Ricchelli F, Piazzesi A, Barel A, Salvato B
Biochem J. 1984 Aug 1;221(3):911-4. doi: 10.1042/bj2210911.
The two copper ions bound in the active site of Octopus vulgaris haemocyanin can be removed by cyanide. The two metal ions react with the ligand sequentially. In this paper the preparation of Octopus half-apo-haemocyanin, containing at the active site a single copper ion, is described. Moreover, the conditions to obtain Octopus apo-haemocyanin, containing less than 3% of copper still bound, are given.
普通章鱼血蓝蛋白活性位点结合的两个铜离子可被氰化物去除。这两个金属离子与配体依次反应。本文描述了制备在活性位点含有单个铜离子的普通章鱼半脱辅基血蓝蛋白的方法。此外,还给出了获得仍结合少于3%铜的普通章鱼脱辅基血蓝蛋白的条件。