摘要
以意大利蜜蜂蛹冻干粉为研究材料,经提取、盐析、浓缩、透析和DEAE纤维素离子交换柱层析等纯化步骤,获得了一种超氧化物歧化酶(SOD)。该酶蛋白结晶呈菱形,PAGE法显示为均一的蛋白谱带。在相同时间内,测定了pH值、温度对该酶活力的影响。结果表明:意大利蜜蜂蛹中SOD在pH值为8.3时,酶活力最高,pH值高于或低于8.3时,酶活力均有明显下降;温度在25℃左右时,该酶活力最高,40℃时保持活力在80%以上,到90℃时没有活力,说明意大利蜜蜂蛹SOD是一种比较耐热的酶,这为SOD的提取提供了新酶源。
In the paper, the freeze-drying pupae of Ap/s mellifer was used as experimental material based on former studies. The purified superoxide dismutase（SOD） was obtained thruogh the extraction, prieipitation, condensation, dialysis and DEAE-cellulose cloumn chromatography and so on. The superoxide dismutaac was rhombus crystal and the PAGE electropherogram showed that it was a homogeneous protein. The result of the influence of enzyme at the different pH and temperature in the same time respectively showed the superoxide dismutase kept the most activity at pH 8.3 and the activity came down above or below pH 8.3. It kept the most activity at the 25 ℃ and it could remain 80% enzyme activity at the 40℃, but it losted the activity in the 90 ℃. So the SOD was a more heat-resistant enzyme. It can afford a new enzyme source of superoxide dismutase extraction.
出处
《安徽农业科学》
CAS
北大核心
2006年第23期6132-6133,共2页
Journal of Anhui Agricultural Sciences
