对生玉米5-氨基酮戊酸脱水酶的简单快速纯化

A Simple Rapid Purification Scheme

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。

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.