Salvato B, Ghiretti-Magaldi A, Ghiretti F
Biochemistry. 1979 Jun 26;18(13):2731-6. doi: 10.1021/bi00580a007.
In the presence of 3 M urea Octopus vulgaris (Mollusca) hemocyanin dissociates completely, giving a single functional component which reassociates in the original aggregate after removal of urea. The molecular weight of this subunit has been determined by gel filtration, by viscosity measurements, and by ultracentrifugation. The values obtrained with the different methods range from 247,000 to 262,000. Electron microscopy shows that the reassociation of the functional subunit after removal of urea is complete and gives the typical cylindrical structure of the native protein. This component is the minimal functional subunit which can be obtained from Octopus hemocyanin without splitting covalent bonds. It is suggested that this component is made by five protomers (50,000 daltons) containing one oxygen binding site each bound covalently through, perhaps, the carbohydrate moieties of the protein.
在3M尿素存在的情况下，普通章鱼（软体动物）血蓝蛋白会完全解离，产生单一的功能成分，去除尿素后该成分会重新结合成原来的聚集体。这个亚基的分子量已通过凝胶过滤、粘度测量和超速离心法测定。用不同方法得到的值在247,000到262,000之间。电子显微镜显示，去除尿素后功能亚基的重新结合是完全的，并呈现出天然蛋白质典型的圆柱形结构。这个成分是可以从章鱼血蓝蛋白中获得的最小功能亚基，且不涉及共价键的断裂。有人提出，这个成分由五个原体（50,000道尔顿）组成，每个原体含有一个氧结合位点，可能通过蛋白质的碳水化合物部分共价结合。
