Gärtner A, Hartmann H J, Weser U
Biochem J. 1984 Jul 15;221(2):549-51. doi: 10.1042/bj2210549.
On the basis of the thermal stability of erythrocuprein (Cu2Zn2-superoxide dismutase) a rapid preparation technique was devised and successfully employed to isolate this protein. Partial heat-deterioration of the haemolysate and subsequent chromatography of the supernatant on DEAE-Sephacel and Sephadex G-75 yielded an electrophoretically homogeneous protein within a few days. The physicochemical properties and biochemical function were identical with those reported for Cu2Zn2-superoxide dismutases prepared by established methods.
基于红细胞铜蛋白(Cu2Zn2 - 超氧化物歧化酶)的热稳定性,设计并成功采用了一种快速制备技术来分离这种蛋白质。对溶血产物进行部分热降解,然后将上清液在DEAE - 葡聚糖凝胶和葡聚糖凝胶G - 75上进行层析,在几天内得到了电泳纯的蛋白质。其物理化学性质和生化功能与通过既定方法制备的Cu2Zn2 - 超氧化物歧化酶所报道的性质相同。