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作 者:黄巨富[1] 汪道涌[1] 汪志平[1] 骆爱玲[1] 顾淑荣[1] 李佳格
机构地区:[1]中国科学院植物研究所
出 处:《Acta Botanica Sinica》1998年第9期880-882,共3页Acta Botanica Sinica(植物学报:英文版)
基 金:国家自然科学基金;国家空间计划资助
摘 要:棕色固氮菌(OP)体内的固氮酶钼铁(MoFe)蛋白和细菌铁蛋白均为重要的生物功能蛋白。前者为生物固氮的关键酶[1],后者则可为生物代谢贮存丰富而又可溶的铁原子[2]。因而都得到了广泛而深入的研究。Kim[3]报道了MoFe蛋白衍射结果。赵宝光等[2]...MgCl 2 was added to the supernatant of the first crystallization of MoFe protein to give a final concentration of 14.6 mmol/L, followed by centrifugation. The treated supernatant solution and MoFe protein could be crystallized by using method of siting drop with PEG 6000 and MgCl 2 as a precipitant and salt,respectively. The larger crystal from the supermatant was observed when the final concentration of PEG and MgCl 2 was 4.5% and 15.6 mmol/L, respectively; but small crystal was observed when the concentration was 0 and 23.8 mmol/L, respectively. The larger crystal in brown rectangular prism of MoFe protein was also obtained using the same crystallization method when the final concentration of PEG and MgCl 2 was 7.44% and 338.0 mmol/L, respectively. It suggests that the two protein crystals seem to be different, the former being bacterioferritin and the later as nitrogenase MoFe protein.
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