| 带羟乙基侧臂三脚架多胺Cu(Ⅱ)配合物切割肌红蛋白所得片断的质谱指认 |
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| 引用本文： | 蒋疆,赵春梅,洪瑾,唐惠炜,朱龙根. 带羟乙基侧臂三脚架多胺Cu(Ⅱ)配合物切割肌红蛋白所得片断的质谱指认[J]. 无机化学学报, 2007, 23(2): 243-252 |
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| 作者姓名： | 蒋疆 赵春梅 洪瑾 唐惠炜 朱龙根 |
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| 作者单位： | 1. 福州大学化学化工学院,福州,350002;南京大学配位化学国家重点实验室,南京,210093
2. 南京大学配位化学国家重点实验室,南京,210093 |
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| 摘 要： | 采用电喷雾质谱和串联质谱以及聚丙烯酰胺凝胶电泳技术研究了[CuL(H2O)](BF4)2(L为2-[二(2-氨乙酸)氨基]乙醇)与马心肌红蛋白的键合作用和水解切割。聚丙烯酰胺凝胶电泳研究显示在中性及60 ℃条件下，切割效率与[CuL(H2O)]2+的浓度和温育时间密切相关。电喷雾质谱和串联质谱分析显示，[CuL(H2O)]2+通过与肌红蛋白的氨基酸His36，His93，His116和Arg139侧链的结合，并在羟乙基侧臂的促进下，选择性地水解了肽键Phe33-Thr34，Gln91-Ser92，Ala94-Thr95，His116-Ser117和Asn140-Asp141。
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| 关 键 词： | 肌红蛋白； 质谱； Cu(Ⅱ)配合物； 切割 |
| 文章编号： | 1001-4861(2007)02-0243-10 |
| 修稿时间： | 2006-09-27 |
Mass Spectrometry Assisted Assignments of Fragments of Myoglobin Cleaved by Copper(Ⅱ) Complex with Tripodal Polyamimine Bearing an Hydroxyethyl Pendant |
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| JIANG Jiang,ZHAO Chun-Mei,HONG Jin,TANG Hui-Wei and ZHU Long-Gen. Mass Spectrometry Assisted Assignments of Fragments of Myoglobin Cleaved by Copper(Ⅱ) Complex with Tripodal Polyamimine Bearing an Hydroxyethyl Pendant[J]. Chinese Journal of Inorganic Chemistry, 2007, 23(2): 243-252 |
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| Authors: | JIANG Jiang ZHAO Chun-Mei HONG Jin TANG Hui-Wei ZHU Long-Gen |
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| Affiliation: | College of Chemistry and Chemical Engineering, Fuzhou University, Fuzhou 350002;State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing 210093,State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing 210093,State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing 210093,State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing 210093 and State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing 210093 |
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| Abstract: | The bonding interaction and hydrolytic cleavage of horse heart myoglobin with [CuL(H2O)](BF4)2, where L is 2-[bis(2-aminoethyl)amino]ethanol, were investigated by electrospray ionization mass spectrometry(ESI-MS), tandem mass spectrometry(MS/MS) and SDS-PAGE electrophoresis. The SDS-PAGE electrophoresis showed that the cleavage yield was dependent on the concentration of [CuL(H2O)]2+ and incubation time. The ESI-MS and MS/MS analysis revealed that with the assistance of the pendant hydroxyl group in [CuL(H2O)]2+, [CuL(H2O)]2+ may selectively hydrolysis the peptide bonds of Phe33-Thr34, Gln91-Ser92, Ala94-Thr95, His116-Ser117 and Asn140-Asp141 of myoglobin by the binding of [CuL(H2O)]2+ to the side chains of His36, His93, His116 and Arg139 of myoglobin. |
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| Keywords: | myoglobin mass spectrometry cleavage |
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