| 小麦胆色素原脱氨酶的电泳性质分析 |
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| 引用本文： | 范军,郭蔼光.小麦胆色素原脱氨酶的电泳性质分析[J].安徽农业大学学报,1998,25(4):429-432. |
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| 作者姓名： | 范军 郭蔼光 |
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| 作者单位： | [1]安徽农业大学生物技术研究中心 [2]西北农业大学基础科学系 |
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| 摘 要： | 经反应红１２０亲和层析纯化的小麦胆色素原脱氨酶（Ｐｏｒｐｈｏｂｉｌｉｎｏｇｅｎ ｄｅａｍｉｎａｓｅ，ＰＢＧＤ，ＥＣ．４，３，１，８），在ＳＤＳ－ＰＡＧＥ和ＩＥＦ－ＰＡＧＥ上均显示一条带，表明已ＰＢＧＤ纯化至均一，它的亚基分子量３６ＫＤ，ｐＩ为４．８。酶活性染色呈一条带，表明无同工酶存在。ＰＡＧＥ显示两条带，证明小麦幼苗中存在酶与底物结合的中间物。脲梯度电泳呈现之字形，在４ｍｏｌ／Ｌ的脲浓度下可使酶
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| 关 键 词： | 胆色素原脱氨酸 凝胶电泳 小麦 电泳性质 |
The Characteristic Assay by Electrophoresis of Porphobilinogen Deaminase from Wheat |
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| Fan Jun.The Characteristic Assay by Electrophoresis of Porphobilinogen Deaminase from Wheat[J].Journal of Anhui Agricultural University,1998,25(4):429-432. |
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| Authors: | Fan Jun |
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| Abstract: | The result of SDS-PAGE and IEF-PAGE analysis confirmed that the extract of porphobilinogen deaminase (PBGD,EC.4.3.1.8.) was homogeneous after purified by Reactive Red 120 affinity chramotography.This deaminase had a subunit of Mr 36 KD with pI 4 8.Nondenaturing PAGE showed two bands,indicating that PBGD can bind PBG to form intermediate complexes,which can be disrupted by urea of 4 mol/L.There appeared only one band in ewzymatic activity,indicating that this enzyme has no isozyme. |
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| Keywords: | Porphobilinogen deaminase (PBGD) PAGE Urea gradient PAGE |
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