Ultraviolet difference spectrl studies of conalbumin complexes with transition metal ions.
Ultraviolet difference spectrl studies of conalbumin complexes with transition metal ions.
复制标题
伴清蛋白与过渡金属离子复合物的紫外差光谱研究。
DOI：
10.1021/bi00837a033
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发表时间：
1969
期刊：
影响因子：
2.9
通讯作者：
R. Woodworth
中科院分区：
文献类型：
--
作者：
A. Tan;R. Woodworth
材料和方法伴清蛋白按先前报道的方法（Woodworth和Schade，1959）制备，但改进之处在于蛋白质在CM-Sephadex C-50柱上层析而不是在CM-纤维素柱上层析。通过分光光度法和金属结合标准，发现该制剂是纯的，并且在聚丙烯酰胺凝胶电泳中是均匀的（Woodworth和Clark，1967）。化学品为试剂级，不经进一步纯化即可使用。CM-Sephadex C-50得自Pharmacia Fine Chemicals，New Market，N。玻璃蒸馏水用于制备所有溶液和稀释液。储备金属离子水溶液在CuCl 2、Zn（Ac）2、MnCl 3中为0.02 μ m。NiS 〇 4、CdCl 2、CoCl 2、CrCl 3和Fe（NH 4）2-（S 〇 4）2。
Materials and MethodsConalbumin was prepared as previously reported (Woodworth and Schade, 1959) with the modification that the protein was chromatographed on a column of CM-Sephadex C-50 rather than CM-cellulose. The preparation was found to be pure by spectrophotometric and metal-binding criteria and to be homogeneous on electrophoresis in polyacrylamide gel (Woodworth and Clark, 1967). Chemicals were reagent grade and were used without fur-ther purification. CM-Sephadex C-50 was obtained from Pharmacia Fine Chemicals, New Market, N. J. Glass-distilled water was used for making all solutionsand dilutions. Stock aqueous metal ion solutions were 0.02 m in CuCb, Zn (Ac),, MnCl ท,. NiS04, CdCL ป, CoCl ท,, CrCl3, and Fe (NH ท,),-(S04) 2.