摘要
采用加热、盐析及DEAE－SephadexA－50柱层析的方法，从扇贝内脏团中分离得到一种高等电点的超氧化物歧化酶（SOD）。该酶由281个氨基酸组成，等电点为8．30。纯酶的比活为2616．4U／mg蛋白（邻苯三酚自氧化法），最大紫外吸收峰270．5nm，为Cu．Zn－SOD，由一个亚基组成，亚基分子量为15000Dr。此外还研究了该酶其他的理化性质。
Cu.Zn-superoxide dismutase with high isoelectric point was isolated from scallop visceral mass by heat treatment, followed by precipitation with ammonium sulfate and column chromatography. The purfied enzyme consisted of 281 amino acid residues. Determined by the autoxidation of pyrogalloy method, its specific activity was 2 616. 4U/mg. It had two 15 KD homogenous subunits. its pI was 8. 3, and maximal ultraviolet absorption peak was at 270. 5nm.Other characteristics of the purfied enzyme were also analyzed.
出处
《海洋水产研究》
CSCD
1998年第2期69-75,共7页
Marine Fisheries Research
基金
1995~1998山东省科委青岛市科委科学基金
关键词
扇贝内脏团
超氧化物歧化酶
纯化
Scallop visceral mass Superoxide dismutase Purification
