期刊文献+

纳米聚硫堇修饰电极的制备及其用于检测血红蛋白的研究 被引量:3

Preparation of poly(thionine) nanoparticles modified electrode and its application to determine hemoglobin
下载PDF
导出
摘要 该文报道了硫堇(Tn)在玻碳电极上的电化学聚合,用原子力显微镜,紫外可见光谱,傅立叶红外变换光谱等手段对纳米聚硫堇进行了表征;研究了纳米聚硫堇修饰电极的电化学性质及血红蛋白在该修饰电极上的直接电化学行为。实验结果表明,纳米聚硫堇修饰电极对血红蛋白(Hemoglobin,Hb)的还原具有催化作用,且还原峰电流与被测蛋白质浓度呈良好线性关系。流动注射分析结果进一步表明该纳米修饰电极具有高的稳定性和好的重现性,用该法测定人体血液中血红蛋白,获得了满意的结果。 A poly(thionine) nanoparticles modified glassy carbon electrode had been prepared by a novel two-step eleetrepolymerization method. Atomic force microscopy (AFM), UV-vis spectrum and Fourier Transform Infrared Spectrometry (FTIR) were used to evaluate poly(thionine) nanoparticles. The electrochemical properties of poly (thionine) nanoparticles as well as the electrochemical behaviors of hemoglobin(Hb) on PTn/GCE had been studied. The results showed that the modified electrode exhibited significantly electroeatalytie activity for the reduction of Hb, and the reduction currents were linear to the concentrations of Hb in aqueous solutions. In addition, the results of flow injection analysis (FIA) further suggested high stability and reproducibility of PTn/GCE and this method was applied to the determination of hemoglobin (Hb) of whole blood.
出处 《化学传感器》 CAS 2004年第4期17-24,共8页 Chemical Sensors
基金 国家自然科学基金(No.20175006)资助项目
  • 相关文献

参考文献15

  • 1李林.蛋白质组学的进展[J].生物化学与生物物理进展,2000,27(3):227-232. 被引量:58
  • 2Zhu Y C,Cheng G J,DoIlg S J.Structural electrochemical study of hemoglobin by in situ circular dichroism thin layer spectroelectrochemistry[J].Biophysical Chemistry,2002,97:129—138.
  • 3Huang H,Hu N F,Zeng Y H,et al.Electrochemistry and electrocatalysis with heme proteins in chitosan biopolymer films[J].Analytical Biochemistry,2002,308:141-151.
  • 4Shen L,Hu N F.Heine protein films with polyami.doamine dendrimer:direct electrochemistry and electrocatalysis[J].Biochimica et Biophysica Acta,2004,1 608:23-33.
  • 5Reed D E,Hawkridge F M.Direct electron transfer reactions of cytochrome C at silver electrodes[J].Anal.Chem.,1987,59(19):2 334.2 339.
  • 6Taniguehi I,Watanabe K,Tominaga M,et al.Direct electron transfer of horse heart myoglobin at an indium oxide electrode[J].J.Ehctroanal.Chem.,1992,333:331-338.
  • 7Rusling J F.Enzyme Bioelectrochemistry in Cast Biomembrane-Like Films[J].Acc.Chem.Res.,1998,31(6):363—369.
  • 8韩吉林,经卫,陈洪渊.生物分子电催化的研究(Ⅲ)——血红蛋白在甲酚固紫修饰碳糊电极上的电催化[J].高等学校化学学报,1993,14(3):332-333. 被引量:8
  • 9李根喜 方惠群 等.分析化学进展[M].南京:南京大学出版社,1994.718.
  • 10冶保献,方程,周性尧.血红蛋白在裸银电极上的光谱电化学研究[J].高等学校化学学报,1998,19(9):1405-1407. 被引量:8

二级参考文献46

  • 1冶保献,周性尧.血红蛋白在裸银电极上的直接电化学及其分析应用[J].高等学校化学学报,1996,17(1):33-37. 被引量:11
  • 2[1]Bianco P, Taye A, Haladjian J. Incorporation of cytochrome c and cytochrome c3 within poly(ester sulfonic acid) films on pyrolytic graphite electrodes[J]. J Electroanal Chem, 1994, 377:299
  • 3[2]Armstrong F A. Probing metalloproteins by voltammetry[M]∥Bioinorganic chemistry, structure and bonding 72. Berlin: Springer-Verlag, 1990:137
  • 4[3]Kassner R J. Effects of nonpolar environments on the redox potentials of heme complexes[J]. Proc Natl Acad Sci USA, 1972, 69:2263
  • 5[4]Hildebrandt P, Stockburger M. Cytochrome c at charged interfaces 1: confomational and redox equilibria at the electrode/electrolyte interface probed by surface-enhanced resonance Raman spectroscopy[J]. Biochemistry, 1989, 28:6710
  • 6[5]Huang Z, Feng M, Wang Y, et al. The direct electrochemistry of cytochrome c in the presence of various amino acids[J]. J Electroanal Chem, 1996, 416:31
  • 7[6]Hu Naifei, Rusling J F. Electrochemistry and catalysis with myoglobin in hydrated poly(ester sulfonic acid) ionomer films[J]. Langmuir, 1997, 13:4119
  • 8[7]Yang Jing, Hu Naifei, Rusling J F. Enhanced electron transfer for hemoglobin in poly(ester sulfonic acid) films on pyrolytic graphite electrodes[J]. J Electroanal Chem, 1999, 463:53
  • 9[8]Murray R W. Chemically modified electrodes[M]∥Bard A J. Electroanalytical chemistry: Vol 13. New York: Marcel Dekker, 1984:191-368
  • 10[9]Bond A M. Modern polarographic methods in analytical chemistry[M]. New York: Marcel Dekker, 1980

共引文献102

同被引文献50

引证文献3

二级引证文献6

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部