Hemocyanin of Octopus vulgaris. The molecular weight of the minimal functional subunit in 3 M urea.
Hemocyanin of Octopus vulgaris. The molecular weight of the minimal functional subunit in 3 M urea.
复制标题
普通章鱼的血蓝蛋白。
DOI：
10.1021/bi00580a007
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发表时间：
1979
期刊：
影响因子：
2.9
通讯作者：
F. Ghiretti
中科院分区：
文献类型：
--
作者：
B. Salvato;A. Ghiretti;F. Ghiretti
在3 M尿素的存在下，章鱼（软体动物）血蓝蛋白完全解离，得到一个单一的功能成分，在去除尿素后重新结合在原来的聚集体。该亚基的分子量已通过凝胶过滤、粘度测量和超离心测定。用不同的方法得到的值范围从247，000到262，000。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，并给出了天然蛋白质的典型圆柱形结构。该组分是可以从章鱼血蓝蛋白中获得的最小功能亚基，而不裂解共价键。有人认为，这一组成部分是由五个原聚体（50，000道尔顿）含有一个氧结合位点，每个结合位点可能通过蛋白质的碳水化合物部分共价结合。
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.