CAJ | 학술논문

以新鲜猪血为原料,首次利用改进的新工艺提取分离超氧化物歧化酶,经过溶血,热变,丙酮沉淀,超滤浓缩,SephadexG-75凝胶过滤层析和DEAE-sepharose-fast flow离子交换层析纯化,冷冻干燥等步骤,得到高纯度酶,并对酶的相关性能进行研究.试验结果显示产品粗酶活性在3 000 U/mg左右,分剐经SephadexG-75和DEAE-sepharose-fast flow层析纯化后,酶活分别达到5 585 U/mg和6 148 U/mg产品得率分别为13.4%和10.32%,SDS-PAGE凝胶电泳显示为单一条带达到电泳纯,其分子量在31 kD附近,其临苯三酚抗氧化活性明显.
이신선저혈위원료,수차이용개진적신공예제취분리초양화물기화매,경과용혈,열변,병동침정,초려농축,SephadexG-75응효과려층석화DEAE-sepharose-fast flow리자교환층석순화,냉동간조등보취,득도고순도매,병대매적상관성능진행연구.시험결과현시산품조매활성재3 000 U/mg좌우,분과경SephadexG-75화DEAE-sepharose-fast flow층석순화후,매활분별체도5 585 U/mg화6 148 U/mg산품득솔분별위13.4%화10.32%,SDS-PAGE응효전영현시위단일조대체도전영순,기분자량재31 kD부근,기림분삼분항양화활성명현.
The Superoxide dismutase(SOD)was extracted from fresh pig blood by improved process via the key step such as hemolysis,heat denaturation,ultrafiltration concentration,lyophilization,sephadexG-75 gel permeation chromatography and DEAE-sepharose-fast-flow ion-exchange chromatography.High purity enzyme was obtained and the related properties were studied.The results showed that the activity of the rude enzyme is about 3 000 U/mg,its activity reaches 5 585 U/mg,6 148 U/mg and the yield rate is 13.4%,10.32%after the sephadexG-75gel permeation chromatography and DEAE-sepharose-fast-flow ion-exchange chromatography,respectively.A sole proteinase belt was observed and its molecular weight is about 31 kD with SDS-PAGE electrophoresis,and the pyrogallol oxidation resistance performed obviously.