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芦荟超氧化物歧化酶同工酶Ⅰ的分离纯化及部分性质 被引量:1

Isolation,Purification and Some Properties of the Isozyme Ⅰ of Superocide Dismutase in Aloe
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摘要 将从芦荟叶中提取的SOD溶液,通过丙酮沉淀、热变性、DEAE-琼脂糖柱层析s、ephacryl S-200凝胶过滤,获得芦荟超氧化物歧化酶同工酶Ⅰ电泳纯产品Fe-SOD。该同工酶经凝胶过滤测定全分子量为46 kD及SDS-PAGE测得亚基分子量为23 kD,由2个亚基组成。经等电点聚焦电泳测得该SOD酶同工酶Ⅰ的等电点为pH8.9。 Superocide dismutase solution extracted from the leaves of the aloe has been isolated and purified by precipitation of actone, denaturization with hearing, DEAE-sepharose column chromatography and Sephacryl S-200 gel giltration. The purified isozyme Ⅰ of superoxide dismutase was homogeneous as shown in SDS-polyacrylamide gel electrophoresis and isoelectric focusing electrophoresis. The molecular weight of the isozyme Ⅰ of superoxide dismytase detemined by gel filtration was 46 kD and SDS-polyacrylamide gel electrophoresis was 23 kD. Isoelectric point of the isozyme Ⅰ of superoxide dismytase was pH 8.9.
出处 《西北农业学报》 CAS CSCD 北大核心 2006年第4期156-159,共4页 Acta Agriculturae Boreali-occidentalis Sinica
关键词 中华芦荟 Fe-SOD纯化 性质 Alone [Aloe vera var. chinensis (Haw) Berg. ] The isozyme Ⅰ of iron-superoxide dismutase Purigication Properties
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