請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/34352
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 張煥宗(Huan-Tsung Chang) | |
dc.contributor.author | Yu-Fen Huang | en |
dc.contributor.author | 黃郁棻 | zh_TW |
dc.date.accessioned | 2021-06-13T06:04:24Z | - |
dc.date.available | 2006-06-21 | |
dc.date.copyright | 2006-06-21 | |
dc.date.issued | 2006 | |
dc.date.submitted | 2006-06-16 | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/34352 | - |
dc.description.abstract | 近年來人類基因體的成功定序,加速了蛋白質體學的蓬勃發展。毛細管電泳具備快速、高效能及樣品消耗量少等優點,在蛋白質分析上,已成為一項不可或缺的重要工具。另外,當材料縮小至奈米尺度時,由於比表面積的增加,量子化侷限效應的產生,往往會展現出與塊材截然不同的物理、化學性質。以金奈米粒子為例,除了具有極佳的生物相容性,在可見光波段的表面電漿共振吸收,也會隨著粒俓大小、形狀、表面環境介電常數以及聚集程度的不同而改變,呈現出肉眼即可辨識的顏色變化。本論文中,我們以毛細管微胞電層析(micellar electrokinetic capillary chromatography)搭配雷射誘導原生螢光偵側系統,有效的分離牛血清蛋白(bovine serum albumin)之水解產物,藉此可成功地觀察胰蛋白酶(trypsin)與金奈米粒子結合後(AuNP-trypsin)其酵素活性的改變。同時以毛細管區帶電泳(capillary zone electrophoresis)檢視AuNP-trypsin水解牛血清蛋白的動力學過程發現,AuNP-trypsin的酵素活性可能因為蛋白質構型(conformation)的改變,而有下降的趨勢。
此外,我們開發出一種微量蛋白質的線上濃縮和分離之技術,來解決一般毛細管電泳,偵測靈敏度不足的問題;藉由高電滲透流引入黏滯度較高的中性聚合物溶液(聚環氧乙烷,簡稱PEO),使得在Tris-borate (pH 10.0)條件下,帶負電的蛋白質由樣品區帶進入PEO溶液時,因電泳遷移率的下降,在兩溶液的界面形成堆積,達到濃縮大體積(1.0 μL)樣品的目的。實驗中發現,樣品注入前,引入一小段十二烷硫酸納(sodium dodecyl sulfate,簡稱SDS, 0.2%),以及添加少許SDS或PEO(0.01%)於樣品區帶,皆有助於減少蛋白質在毛細管表面的吸附,在分析6種蛋白質之混合樣品時,可解析出12根微異質性(microheterogeneity)蛋白質訊號峰。另外,此方法對蛋白質的濃縮倍數高達84倍,以α-lactalbumin為例,偵測極限可降至0.5 nM。這項技術可直接偵測未經前處理的人體尿液中所含之人血清蛋白(human serum albumin),其含量為0.18(± 0.04)μM,以及50個紅血球萃取液中的血紅素(hemoglobin),其含量為45(± 3)nM,其實際樣品偵測值皆符合文獻報導。 論文中,我們亦提出一套簡單的合成技術。在鹼性條件下(pH > 8.0)合成出形狀多樣且產率、純度(> 90%)相當高的金–銀奈米球、奈米棒和奈米線。不同反應時間、pH、胺基酸溶液的種類、濃度之選擇,會影響維他命C(ascorbic acid)還原金、銀離子以及十六烷基三甲基溴化銨(cetyltrimethylammonium bromide)穩定金–銀奈米粒子不同晶格面結構之能力。在pH = 8.0、9.0和10.0的甘胺酸(glycine,0.1 M)溶液中,分別可合成出棒狀、啞鈴型和球型金–銀奈米結構。在0.05 M和0.1 M離胺酸(Lysine,pH 10.0)溶液中,可成功地合成出項鍊型排列的金–銀奈米粒子和奈米線。其餘在組胺酸(histidine,0.1 M,pH 8.0和9.0)和甲硫胺酸(methionine,0.1 M,pH 10.0)溶液中,亦可巧妙的控制花生米和玉黍蜀形狀金–銀奈米材料之合成。 最後,利用金奈米粒子與硫醇間的強鍵結,以及金奈米粒子能吸收紫外光光子並轉換能量至分析物,使之脫附游離的能力,我們以尼羅紅(Nile Red,簡稱NR)修飾金奈米粒子(NRAuNPs)系統,搭配表面輔助雷射脫附游離化質譜技術,可在不受到生物體樣品中複雜基質的干擾下,成功地選擇性分離並定量出紅血球萃取液和血漿樣品中,具有疾病指標的麩胱甘肽(glutathione)和半胱胺酸(cysteine),其含量分別為0.79(± 0.08)mM和11(± 1)μM並符合文獻報導。另外,利用硫醇分子較容易取代NR產物且中和AuNPs表面電荷使AuNPs沈澱的特性,亦可簡單快速地分離硫醇(沈澱)和非硫醇(上層溶液)分子,並達到濃縮硫醇分子的目的,以偵測麩胱甘肽為例,藉由此離心濃縮步驟,可進一步降低麩胱甘肽的偵測極限至25 nM。 | zh_TW |
dc.description.abstract | In order to develop novel analytical techniques for the analysis of biomolecules such as proteins and aminothiol compounds, we take the advantages of high efficiency, rapidity of capillary electrophoresis (CE) and unique optical and large surface properties of nanomaterials. CE in conjunction with laser-induced fluorescence has been separately applied to study the differential activity of enzymes in free solution and those are bound to gold nanoparticles (AuNPs) and improved sensitivity and efficiency for protein analysis. Differently shaped and sized Au-based nanoparticles (NPs) have been prepared and some of them have been tested to be efficient selectors and matrices for aminothiols compounds in surface assisted laser desorption ionization-mass spectrometry (SALDI-MS).
The specificity and activity of trypsin that is conjugated to gold NPs (AuNP-trypsin) for proteins have been investigated by micellar electrokinetic chromatography (MEKC) and capillary zone electrophoresis (CZE) with laser-induced-fluorescence (LIF) detection. In the presence of sodium dodecyl sulfate (SDS), adsorption of the tryptic fragments on AuNP-trypsin and on the capillary wall is reduced. Thus, the sensitivity and resolution of the tryptic fragments from bovine serum albumin (BSA) is improved. According to the electropherograms, the activity of AuNP-trypsin is lower than that of free trypsin. It is suggested that changes in the conformations and steric effects contribute to the loss of activity and changes in specificity of trypsin adsorbed on AuNPs. An on-line concentration and separation method for analyzing large-volume protein samples by CE-LIF is described. After the injection of 1.0-μL samples, proteins migrate against the electroosmotic flow (EOF) and enter the poly(ethylene oxide) (PEO) zone; this process causes them to slow down and stack at the boundary between the PEO. Either 0.01% SDS or 0.01% PEO was used as sample additives to improve the stacking and separation efficiencies. By applying a short plug of 0.2% SDS prior to sample injection, the microheterogeneity of the proteins can be resolved. 12 peaks are detected when injecting 1.0-μL of sample containing six model proteins (0.1 μM). The limit of detection (LOD) for α-lactalbumin is 0.5 nM, which is an 84-fold sensitivity enhancement over the traditional method. Preparation of Au core–Au–Ag shell NPs in different morphologies can be easily achieved by controlling both the pH and the glycine concentration. Using a seed–growth method, we prepared high-quality Au–Ag NPs from a glycine solution under alkaline conditions (pH > 8.5). Dumbbell- and peanut-shaped Au core–Au–Ag shell NPs were prepared in aqueous solution at the concentrations of glycine greater than 0.5 M and greater than 0.2 M at pH 9.5 and 10.5, respectively. In addition, we were able to affect the shapes and sizes of the Au–Ag NPs by controlling the reaction time. At pH 9.7, we observed the changes in the morphologies of the Au core–Au–Ag shell NPs—from regular (rectangular) to peanut- and dumbbell-shaped, and finally to jewel-, diamond-, and/or sphere-shaped—that occurred during the course of a 60-min reaction. We further prepared differently shaped and sized Au–Ag nanocomposites from gold nanorod (AuNR) seeds in various amino acid solutions at the pH values ranging over 8.0–11.5. Our study shows that the pH as well as the concentration and species of amino acids have great impacts on the preparation of I-liked, dumbbell-liked, sphere-liked, peanut-liked, and corn-liked NPs as well as nanowires (NWs), mainly through the control of the reducing ability of ascorbate (or amino acids), oxidizing abilities of Au and Ag ions, and/or recognition capability as well as surface charges of the amino acids on the AuNRs. Depending on the value of pH, we were able to prepare I-shaped, dumbbell-shaped, and/or sphere-shaped Au–Ag nanocomposites in 0.1 M solutions of Arg, Gly, Glu, Gln, Lys, and Met. In His solutions at pH 8.0 and 9.0, we obtained peanut-shaped Au–Ag nanocomposites. Corn-shaped Au–Ag nanocomposites were prepared in 0.1 M Met solutions (pH 9.0 and 10.0). By controlling the Lys concentration at pH 10.0, we synthesized pearl-necklace-shaped Au–Ag nanoparticles and Au–Ag wires. Nile Red-adsorbed AuNPs (NRAuNPs) has been demonstrated as selective probes and matrices for the determination of aminothiols through SALDI-MS. Due to the high specificity of NRAuNPs toward thiol-containing compounds as well as the aggregation induced by the binding of these molecules to the surfaces of NRAuNPs, NRAuNPs are capable to selectively concentrate three aminothiols—glutathione (GSH), cysteine (Cys), and homocysteine (HCys) in the precipitate—from a mixtures containing four amino acids. The preconcentration approach also provides an LOD of 25, 54, and 34 nM, for the determinations of GSH, Cys, and HCys, respectively. This method was validated in the analyses of GSH in red blood cells and of Cys in plasma and has great potential for diagnosis. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T06:04:24Z (GMT). No. of bitstreams: 1 ntu-95-F91223005-1.pdf: 4221872 bytes, checksum: cfe98b90c0997efee480862afdc283fa (MD5) Previous issue date: 2006 | en |
dc.description.tableofcontents | 中文摘要 І
Abstract III Contents VI Table Contents X Figure Contents X Conclusions and Prospects 199 Publications 203 1. Introduction 1 1.1 Capillary Electrophoresis 2 1.2 Basic Principles 3 1.2.1 Electrophoretic Mobility 3 1.2.2 Zeta Potential and Electroosmotic Flow 3 1.2.3 Efficiency and Resolution 4 1.3 Capillary Electrophoresis System 5 1.4 Electrophoretic Approaches for Protein Analysis 5 1.4.1 Separation Mechanisms 7 1.4.2 Detection Systems 8 1.4.3 Capillary Coating 9 1.4.4 Separation Techniques 11 1.4.4.1 Zone Electrophoresis 11 1.4.4.2 Isoelectric Focusing 12 1.4.4.3 Micellar Electrokinetic Chromatography 13 1.4.4.4 Sieving Electrophoresis 14 1.4.5 On-line Concentration Techniques 15 1.4.5.1 Field Amplification Stacking 15 1.4.5.2 Isotachophoretic Stacking and Isoelectric Focusing 16 1.4.5.3 pH-mediated Approach 17 1.4.5.4 Sweeping 18 1.5. Nanotechnology 19 1.6. Optical Properties 19 1.7. Architectures 20 1.7.1 Anisotropic Architectures 20 1.7.2 Nanocomposites and Core-Shell Architectures 23 1.7.3 Organization of Au Nanostructures into Macroscopic Architectures 25 1.8. Applications 26 1.8.1 Imaging 26 1.8.2 Sensing 28 1.8.2.1 Colorimetric Assay 28 1.8.2.1.1 Absorbance-Based Assay 28 1.8.2.1.2 Scattering-Based Assay 30 1.8.2.2 Bio-Barcode Assay 31 1.8.2.3 Fluorescence Quenching Assay 32 1.8.3 Nanomaterials in Enzyme Immobilization 33 1.8.4 Nanomaterials in Laser-Desorption/Ionization Mass Spectrometry 34 1.9 Motive of Research 36 1.10 References 37 2. Exploring the Activity and Specificity of Gold Nanoparticle-bound Trypsin by Capillary Electrophoresis with Laser-induced-fluorescence Detection 59 2.1 Introduction 60 2.2 Experimental Section 62 2.2.1 Materials 62 2.2.2 Capillary Electrophoresis Apparatus 62 2.2.3 Synthesis of AuNPs 63 2.2.4 Formation of AuNP-trypsin and AuNP-BSA 64 2.2.5 Tryptic Digestion and Peptide Separation by CE 64 2.2.6 Spectroscopic Measurement 65 2.3 Results and Discussion 65 2.3.1 Effect of Background Electrolyte on Separation 65 2.3.2 Specificity of AuNP-Trypsin and Trypsin 67 2.3.3 Kinetics 69 2.4 Conclusions 70 2.5 References 71 3. On-line Concentration of Microheterogeneous Proteins by Capillary Electrophoresis Using SDS and PEO as Additives 78 3.1 Introduction 79 3.2 Experimental Section 82 3.2.1 Apparatus 82 3.2.2 Chemicals 83 3.2.3 Polymer Solutions 83 3.2.4 Treatment of Capillaries and Separation 83 3.2.5 Urine Analysis 84 3.2.6 Analysis of Human Red Blood Cells (RBCs) 85 3.3 Results and Discussion 85 3.3.1 Generation of Reproducible EOF 85 3.3.2 Optimization of Stacking Efficiency 86 3.3.3 Improved Separation Efficiency 88 3.3.4 Comparison of LIF and UV-Vis Detection 92 3.3.5 Analysis of Large-volume Biological Samples 92 3.4 Conclusions 94 3.5 References 95 4 Preparation of Au Core–Au–Ag Shell Nanorods from Gold Seeds by Controlling Glycine Concentration and pH 108 4.1 Introduction 109 4.2 Experimental Section 111 4.2.1 Chemicals 111 4.2.2 Synthesis of AuNR Seeds 112 4.2.3 Synthesis of Differently Shaped and Sized Au Core–Au–Ag Shell NPs 112 4.2.4 Absorbance, transmission electron microscopy (TEM), and X-ray photoelectron spectra (XPS) measurements 113 4.2.5 Thermogravimetric Analysis (TGA) Measurements 114 4.2.6 Inductively Coupled Plasma-Mass Spectrometry (ICP-MS) Measurements 114 4.2.7 Matrix-assisted Laser Desorption/Ionization Mass Spectrometry (MALDI-MS) Measurement 115 4.2.8 Fourier Transform Infrared (FT-IR) Spectroscopic Measurement 115 4.2.9 Zeta Potential Measurement 115 4.3 Results and Discussion 116 4.3.1 Characterization of the Formation of Au–Ag NPs 116 4.3.2 Effect of Glycine on the Formation of Au–Ag NPs 119 4.3.3 Effect of pH on the Formation of Au–Ag NPs 121 4.3.4 Time Evolution of the Formation of Au–Ag NPs 122 4.4 Conclusions 123 4.5 References 123 5 Growth of Various Au–Ag Nanocomposites From Gold Seeds in Amino Acid Solutions 137 5.1 Introduction 138 5.2 Experimental Section 141 5.2.1 Chemicals 141 5.2.2 Synthesis of AuNR seeds 141 5.2.3 Synthesis of Differently Shaped and Sized Au–Ag Nanocomposites 142 5.2.4 Absorbance and Transmission Electron Microscopy (TEM) Measurements 142 5.2.5 Inductively Coupled Plasma-Mass Spectrometry (ICP-MS) Measurements 143 5.3 Results and Discussion 143 5.3.1 Synthesis of Different Au–Ag Nanocomposites in Various Amino Acid Solutions 143 5.3.2 Nanocomposites Prepared in Lysine Solutions 147 5.3.3 Nanocomposites Prepared in Arginine Solutions 149 5.3.4 Nanocomposites Prepared in Methionine Solutions 151 5.4 Conclusions 152 5.5 References 153 6 Nile Red-Adsorbed Gold Nanoparticle Matrices for Determining Aminothiols Through Surface Assisted Laser Desorption/Ionization Mass Spectrometry 165 6.1 Introduction 166 6.2 Experimental Section 169 6.2.1 Chemicals 169 6.2.2 Synthesis of 14-, 32-, and 56-nm-diameter AuNPs 169 6.2.3 Characterization of AuNPs 169 6.2.4 Preparation of NRAuNPs 170 6.2.5 Preparation of Samples 170 6.2.6 Preparation of Thiol Extracts from Lysed Red Blood Cells (RBCs) and Plasma Samples 171 6.2.7 MALDI-TOF and SALDI-TOF MS Measurements 172 6.3 Results and Discussion 172 6.3.1 NRAuNPs as Assisted Matrices for SALDI-MS Analysis 172 6.3.2 Effects of Particle Size and Concentration 174 6.3.3 Effects of pH and Choice of Buffer Solution 176 6.3.4 Quantitative Analyses of Three Model Thiols 177 6.3.5 Trapping Capacity of NRAuNPs 179 6.3.6 Determination of GSH, Cys, and HCys in Blood Samples 181 6.4 Conclusions 183 6.5 References 184 Table Contents Table 3.1 Chemical and Physical Properties of Proteins 99 Table 3.2 Comparison of Migration Times, Peak Heights, and Resolutions for Proteins Prepared in Different TB Buffers (pH 10.0) 100 Table 3.3 Impacts of Sample Additives on the Values of Linear Regression (LR), Linear Regression Coefficient (R2), LOD, Sensitivity Enhancement (SE), and Efficiency (N) for Various Proteins 101 Table 4.1 The Physical and Optical Properties of the AuNRs and the Au Core–Au–Ag Shell NPs 126 Table 4.2 The Shapes and Physical Properties of the AuNRs and the Au Core–Au–Ag Shell NPs 127 Table 5.1 Shapes of Au–Ag nanocomposites Prepared in the Presence of Various Amino Acids and at Different Values of pH 156 Table 5.2 ICP-MS Measurements of the Au and Ag Contents of the Corn-Shaped NRs Prepared in 0.1 M Met Solution at pH 10.0 as a Function of Time 157 Figure Contents Figure 1.1 Illustration of double layer and zeta potential (ξ) 54 Figure 1.2 EOF and pumped flow profiles 55 Figure 1.3 Instrumental set-up of a capillary electrophoresis-laser induced fluorescence (CE-LIF) system 56 Figure 1.4 Schematic representation of the principle of MEKC 57 Figure 1.5 Schematic diagram of the principle of sample stacking in FAS 58 Figure 2.1 Effect of background electrolytes on the separation of tryptic digests of BSA by capillary electrophoresis 73 Figure 2.2 Exploring the specificity of AuNP-tryptic and tryptic digests of BSA by capillary electrophoresis 74 Figure 2.3 Effect of SDS on the fluorescence spectra of tryptic and AuNP-tryptic digests of BSA 75 Figure 2.4 Electropherogram and FTIR spectra of tryptic digests of AuNP-BSA 76 Figure 2.5 Electropherograms of tryptic and AuNP-tryptic digests of BSA obtained by CZE-LIF using AB 580 77 Figure 3.1 Effect that SDS addition in samples has on separating 1.0-µL protein samples by CE with LIF detection at 12.5 kV using PEO 102 Figure 3.2 Effect of sample pH on the separation of 1.0-µL protein samples (0.1 µM) by CE with LIF detection at 12.5 kV using PEO 103 Figure 3.3 Separations of 1.0-µL protein samples by CE with LIF detection in the (A) absence and (B, C) presence of an SDS plug (0.2%, ca. 2.5 cm) at 12.5 kV using PEO 104 Figure 3.4 Separation of a 1.0-µL protein sample by CE with UV-Vis detection in the presence of a SDS plug (1.0%, ca. 2.5 cm) at 12.5 kV using PEO 105 Figure 3.5 On-line concentration and separation of a urine sample by CE with LIF detection 106 Figure 3.6 Separation of lysed RBCs samples by CE with LIF detection 107 Scheme 6.1 UV–Vis extinction spectra for the original AuNRs and Au core–Au–Ag shell NPs prepared in different concentrations of glycine solutions under alkaline conditions 128 Scheme 6.2 TEM images of the original AuNR seeds and the Au core–Au–Ag shell NPs obtained from the growth solutions of glycine under alkaline conditions 129 Scheme 6.3 XPS spectra of Ag (3d) and Au (4f) in the Au core–Au–Ag shell NP 130 Scheme 6.4 EDX analysis of the Au core–Au–Ag shell NPs prepared in 0.02 M and 0.05 M glycine solutions at pH 9.5 131 Scheme 6.5 TEM and HR-TEM of representative Au core–Au–Ag shell NP(s) 132 Scheme 6.6 FT-IR spectra of CTAB, glycine, CTAB-modified AuNRs and CTAB and glycine-modified Au core–Au–Ag shell NPs prepared in 0.2 M glycine solution at pH 9.7 133 Scheme 6.7 TGA data of CTAB, glycine, CTAB-modified AuNRs and CTAB and glycine-modified Au core–Au–Ag shell NPs prepared in 0.2 M glycine solution at pH 9.7 134 Scheme 6.8 TEM images and UV–Vis extinction spectra displaying the evolution of the formation of Au core–Au–Ag shell NPs incubated in 0.1 M glycine solution at pH 9.7 as a function of time 135 Scheme 4.1 Morphologies of the Au core–Au–Ag shell NPs prepared under the different conditions 136 Figure 5.1 TEM images of the differently shaped Au–Ag nanocomposites prepared from AuNR seeds in different amino acid solutions (0.1 M) under alkaline conditions 158 Figure 5.2 UV–Vis extinction spectra of the Au–Ag nanocomposites prepared from AuNRs seeds in 0.1 M (A) Gln, (B) His, (C) Lys, and (D) Met solutions under alkaline conditions 159 Figure 5.3 HR-TEM image of the Au–Ag NWs that were prepared from AuNR seeds in 0.1 M Lys solutions at pH 10.0 160 Figure 5.4 TEM images of the Au–Ag nanocomposites from AuNR seeds that were prepared in (A) 0.05, (B) 0.1, and (C) 0.2 M Lys solutions at pH 10.0 161 Figure 5.5 (A) TEM images and (B) UV–Vis extinction spectra displaying the evolution of the formation of Au–Ag NRs incubated in 0.1 M Arg solution at pH 11.5 as a function of time 162 Figure 5.6 HR-TEM image of a dumbbell-shaped Au–Ag NP prepared from AuNR seeds in 0.1 M Arg solution at pH 11.5 163 Figure 5.7 TEM images of Au–Ag nanocomposites prepared from AuNR seeds in 0.1 M Met solution at pH 10.0 164 Figure 6.1 Mass spectra of GSH (1.0 mM) with 14-nm-diameter (NR)AuNPs (1×), AuNPs, and DHB (10 mg/mL) as matrices 189 Figure 6.2 Plot of the intensity ratios of the [GSH + Na]+ and [Au]+ ions against the concentration (0.5–10×) when using the 14-nm-diameter (NR)AuNPs as sample matrices 190 Figure 6.3 Mass spectra of GSH (0.1 mM) at different values of pH and different buffer solutions when using the 14-nm-diameter (NR)AuNPs (3×) as matrices 191 Figure 6.4 Calibration curves of three representative aminothiols. 14-nm-diameter (NR)AuNPs (3×) were used as matrices for the SALDI-MS analyses 192 Figure 6.5 SALDI mass spectra of three mixed aminothiols: GSH (20.0 µM), Cys (40.0 µM), and HCys (40.0 µM). 14-nm-diameter (NR)AuNPs (3×) were used as matrices for these SALDI-MS analyses 193 Figure 6.6 Mass spectra of mixtures of GSH (1.0 and 0.1 µM) with (A, B) 14-nm-diameter (NR)AuNPs (3×) as matrices without concentration of the samples and (C) 0.1× (NR)AuNPs as probes to trap 0.1 µM GSH in aqueous solution (1.0 mL) by a concentration factor of 50× 194 Figure 6.7 Mass spectra of a mixture of arginine (5.0 µM), GSH (5.0 µM), and 14-nm-diameter NRAuNPs (3×) in 0.5 mM ammonium citrate (pH 4.0) 195 Figure 6.8 Mass spectra of GSH in an RBC lysate 196 Figure 6.9 Mass spectra of Cys in a diluted plasma sample 197 Scheme 6.1 Illustrations of the interactions between aminothiols (GSH, Cys and HCys), Arg and NRAuNPs 198 | |
dc.language.iso | en | |
dc.title | 蛋白質之毛細管電泳分析與金奈米粒子之生物應用 | zh_TW |
dc.title | Capillary Electrophoresis for Protein Analysis and Bioapplications of Gold-based Nanoparticles | en |
dc.type | Thesis | |
dc.date.schoolyear | 94-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 劉春櫻(Chuen-Ying Liu),何國榮(Gour-Rong Her),蔡素珍(Suh-Jen Tsai),江旭禎 | |
dc.subject.keyword | 毛細管電泳,金奈米粒子,金-銀奈米粒子,表面輔助雷射脫附游離化質譜, | zh_TW |
dc.subject.keyword | Capillary electrophoresis,gold nanoparticles,gold-silver nanocomposites,SALDI-MS, | en |
dc.relation.page | 205 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2006-06-17 | |
dc.contributor.author-college | 理學院 | zh_TW |
dc.contributor.author-dept | 化學研究所 | zh_TW |
顯示於系所單位: | 化學系 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-95-1.pdf 目前未授權公開取用 | 4.12 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。