| 对生玉米5-氨基酮戊酸脱水酶的简单快速纯化 |
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| 引用本文： | 项艳,范军,朱苏文,李纯,程备久. 对生玉米5-氨基酮戊酸脱水酶的简单快速纯化[J]. 安徽大学学报(自然科学版), 1999, 23(2): 107-110 |
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| 作者姓名： | 项艳 范军 朱苏文 李纯 程备久 |
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| 作者单位： | 安徽农业大学,合肥,230036 |
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| 摘 要： | 以聚乙二醇６０００分级沉淀、ＤＥＡＥ－ＳｅｐｈａｒｏｓｅＣＬ－６Ｂ，ＰｈｅｎｙｌＳｅｐｈａｒｏｓｅ４Ｂ层析和制备电泳初步纯化了对生玉米的５－氨基酮戊酸脱水酶，它在ｐＨ８．５时比活为３１Ｕ／ｍｇ蛋白，酶纯化了１１２倍，得率为１２％，其亚基分子量为４１ＫＤ，它可以用于酶促合成胆色素原，也可用于联合法测定胆色素原脱氨酶的酶活
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| 关 键 词： | 5－氨基酮戊酸脱水酶，胆色素原脱氨酶，对生玉米 |
A Simple Rapid Purification Scheme for 5 - Aminolevulinate Dehydratase from Oppsitefolic Maize Leaves |
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| Affiliation: | (Anhui Agricultural University Hefei 230036 |
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| Abstract: | aminolevulinate dehydratase(ALAD) was purified simply and rapidly from oppsitefolic maize leaves. The procedure contained centrifuge extract,PEG6000 3%-13% fractionation,DEAE Sepharose CL-6B and phenyl Sepharose $B chromatography respectively,and preparative polyacrylamide gel electrophoresis. After it was purified 112 fold and a yield for 12%, ALAD showed a specific activity of 31U/mg protein at pH 8.5. The purified enzyme is not only used for synthesizing PBG but also for couple enzymatic assay of PBGD. It subunit is about 41KD. |
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| Keywords: | Aminolevulinate dehydratase porphobilinogen deaminase oppsitifolic maize |
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