Clinical Chemistry AACC Online Job Center
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 52: 1389-1394, 2006; 10.1373/clinchem.2005.061176
This Article
Right arrow Abstract Freely available
Right arrow Full Text (PDF)
Right arrow 061176.Supplemental Data
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (20)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jiang, Z.
Right arrow Articles by Qin, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jiang, Z.
Right arrow Articles by Qin, A.
Related Collections
Right arrow Automation and Analytical Techniques
(Clinical Chemistry. 2006;52:1389-1394.)
© 2006 American Association for Clinical Chemistry, Inc.

Automation and Analytical Techniques

Gold-Labeled Nanoparticle-Based Immunoresonance Scattering Spectral Assay for Trace Apolipoprotein AI and Apolipoprotein B

Zhiliang Jiang1,2,a, Shuangjiao Sun1, Aihui Liang2, Wenxin Huang1 and Aimiao Qin2

1 Department of Resource and Environmental Science, Guangxi Normal University, Guilin, China.
2 Department of Material and Chemical Engineering, Guilin University of Technology, Guilin, China.

aAddress correspondence to this author at: Department of Resource and Environmental Science, Guangxi Normal University, Guilin 541004, China.


   Abstract
Top
 Abstract
Introduction
 Materials and Methods
 Results and Discussion
 References
 
Background: Apolipoprotein AI (ApoAI) and ApoB are risk indicators of cardiovascular disease. We describe the use of immunoresonance scattering to measure the ApoAI and ApoB in serum.

Methods: We used a trisodium citrate method to prepare 9.0-nm gold nanoparticles labeled with goat anti-human ApoAI and ApoB antibodies. The immune reaction between gold-labeled antibodies and antigens took place in Na2HPO4-NaH2PO4 buffer solution (pH 6.4 for ApoAI and pH 6.0 for ApoB) in the presence of 75 g/L polyethylene glycol (PEG). We used a transmission electron microscope to observe the shape of the gold nanoparticles. Results were compared with those obtained by immunoturbidimetric methods. Twenty-five human serum samples were assayed by the immunoresonance scattering assay preset with the data indicated and by an immunoturbidimetric assay.

Results: The presence of PEG greatly enhanced the intensity of resonance-scattering peaks at 560 nm. The intensity ({Delta}I) was proportional to concentration at 0.00833–0.3333 mg/L ApoAI and 0.00197–0.1972 mg/L ApoB. The detection limits were 2.04 and 0.96 µg/L for ApoAI and ApoB, respectively. The results for human serum samples were in agreement with those obtained with an immunoturbidimetric method. Linear regression analysis revealed a correlation coefficient, slope, and intercept of 0.915, 0.966, and 68.53 mg/L, respectively, for ApoAI and 0.919, 0.996, and 15.46 mg/L for ApoB.

Conclusion: This method showed high sensitivity and good selectivity for quantitative determination of ApoAI and ApoB in human serum, with satisfactory results.


   Introduction
Top
 Abstract
 Introduction
Materials and Methods
 Results and Discussion
 References
 
Apolipoproteins are the protein component of lipoproteins. Apolipoprotein AI (ApoAI)1 is the major protein in HDL (1), and apolipoprotein B (ApoB) is the major protein in LDL. ApoB maintains the structure of proteins, transports lipid, and regulates lipid metabolism(2). ApoAI and ApoB are risk predictors of cardiovascular disease, as are total cholesterol, HDL-cholesterol, and LDL-cholesterol(3)(4). Increased ApoAI is associated with decreased risk of coronary heart disease, whereas increased ApoB is associated with increased risk(5)(6)(7). ApoAI and ApoB are better predictors of cardiovascular disease risk than the corresponding lipoprotein cholesterols(3)(4)(8). Methods for measuring ApoAI and ApoB include radial immunodiffusion(9), enzyme immunoassays(10), radioactivity immunoanalysis(11), ELISA(12), capillary electrophoresis(13), immunonephelometric assays(14), and immunoturbidimetric assays(14). Among these methods, radial immunodiffusion is simple, but it can be time-consuming and unreliable. Compared with other methods, RIA and ELISA are more sensitive and use smaller amounts of antisera, but some of the reagents used are harmful. Immunoturbidimetric assays are simple and rapid, but they require large amounts of antisera and cannot provide measurements at nanogram concentrations. Gold immunolabeling has been applied in medicine and food safety because it is a rapid and simple technique that does not use harmful reagents(15). Resonance scattering (RS) spectral analysis can rapidly analyze nanogram concentrations of proteins(16)(17)(18)(19)(20). Recent studies have shown that liquid-phase gold nanoparticles have a strong resonance-scattering effect(21). We combined an immunoreaction and the resonance-scattering effects of gold nanoparticles to establish a nano-gold-labeled immunoresonance scattering spectral method to quantitatively and qualitatively determine ApoAI and ApoB in human serum.


   Materials and Methods
Top
 Abstract
 Introduction
 Materials and Methods
Results and Discussion
 References
 
reagents and apparatus
We obtained HAuCl4 from the National Pharmaceutical Group Chemical Reagents Company, China. Goat anti-human ApoAI and ApoB antisera, ApoAI, and ApoB were purchased from Shenfeng Biological Reagents Limited Company. We used 0.20 mol/L stock solutions of Na2HPO4 and NaH2PO4 to prepare phosphate buffer (PB) solutions with different pH values. Trisodium citrate, polyethylene glycol (PEG)-6000, PEG-4000, PEG-10000, PEG-20000, and KCl were used. All reagents were of analytical grade, and the water used in experiments was doubly distilled.

For the instrumentation, we used a Model RF-540 spectrofluorometer (Shimadzu), Model 79-1 magnetic heat agitator (Zhongda Instrumental Plant), Model SK8200LH ultrasonic reactor (Kedao Ultrasonic Instrument Limited Company), and Model H-600 transmission electron microscope (Electronic Stock Limited Company).

preparation and identification of colloidal gold
Preparation of colloidal gold.
We used the improved method (22) to prepare colloidal gold by adding HAuCl4 solution to a boiled solution of trisodium citrate while stirring, not following the common, reversed procedure. With this method we obtained gold colloid with a consistent particle size of 8–10 nm.

Identification of colloidal gold.
We used a transmission electron microscope to determine the size and uniformity of the gold particles. Examination of the gold nanoparticles (see Fig. 1 in the Data Supplement that accompanies the online version of this article at http://www.clinchem.org/content/vol52/issue7/) revealed that the size was ~9 nm, and the distribution and size were uniform and consistent. To guarantee gold particle size consistency, we used the same colloidal gold RS characteristic peak intensity of 560 nm for all experiments.


Figure 1
View larger version (94K):
[in this window]
[in a new window]
  		Figure 1. Transmission electron micrograph of gold-labeled goat anti-human ApoAI antiserum and ApoAI system.

Condtions were as follows: PB solution (pH 6.4) containing 23.18 mg/L goat anti-human ApoAI antiserum, 0.17 mg/L ApoAI, and 75 g/L PEG-6000.

preparation of the immuno-gold probe
Pretreatment of goat anti-human apolipoprotein antisera.
Excessive salt lowers the zeta potentiometry of gold particles, influences the absorption of goat anti-human apolipoprotein antisera on gold surfaces, and can lead to aggregation of colloidal gold. We eliminated redundant electrolytes from the apolipoprotein antisera before labeling by dialysis for 30 h in doubly distilled water.

Adjustment of the colloidal gold pH.
Because the combination of colloidal gold with ApoAI and ApoB antisera is done by physical force, successful combination depends on the pH. In this experiment, we used an RS method to test the influence of different pH conditions on colloidal gold labeling. We adjusted the pH in 1.0-mL aliquots of 58 mg/L colloidal gold solution by adding 0.20 mol/L K2CO3 and 0.10 mol/L HCl to each tube and then adding 25 µg of ApoAI antiserum or 25 µg of ApoB antiserum, respectively. After 5 min, we added 0.10 mL of 100 g/L KCl solution; 2 h later, we diluted the solution with doubly distilled water to 3.0 mL. We then used immunoresonance scattering to determine the scattering intensity at 560 nm (23)(24). At a pH <7.0, in the case of ApoAI, the addition of the antisera did not stabilize the gold nanoparticles (see Table 1 in the online Data Supplement). When the pH was >7.0, the intensity decreased and the system stabilized because coating of the gold particles by the ApoAI antisera prevented aggregation of the colloidal gold by the KCl solution. In addition, pH 7.5 optimized labeling of ApoB antisera with colloidal gold (see Table 1 in the online Data Supplement). Before adjusting pH, we used a 1 g/L PEG-20000 to stabilize the colloidal gold(25).

Selection of the ratio between colloidal gold and the antibody.
We added 0, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, and 55 µg of ApoAI and ApoB antisera to 1.0 mL of a 58 mg/L colloidal gold solution. The pH of the colloidal gold solution had been adjusted to 7.0–7.5. After 5 min, we added 0.10 mL of 100 g/L KCl solution and mixed well. After 2 h, we measured the resonance-scattering intensities in each tube. Resonance-scattering intensities were stronger in the tubes with 0–30 µg of antisera than in the tubes with 35–55 µg of antisera, which remained stable (see Table 2 in the online Data Supplement). Thus, 35 µg was the minimum amount of antisera that stabilized 1.0 mL of colloidal gold solution.

Preparation of gold-labeled goat anti-human ApoAI and ApoB antisera.
We adjusted 100 mL of a colloidal gold solution to pH 7.0–7.5. During magnetic stirring, we added 3.5 mg of ApoAI antisera to 100 mL of colloidal gold, maintaining the dropping time for 5 min, and 1.75 mL of 30 g/L PEG-20000 as stabilizer, to a final concentration of ~0.5 g/L. The mixture was stirred for 15 min and kept at 4 °C. The labeling procedures for ApoB antisera were the same as for ApoAI. The gold-labeled antisera were not purified by centrifugation, and the results were consistent with those for purified material. Micrographs of gold-labeled ApoAI antisera (see Fig. 2 in the online Data Supplement) showed that the gold nanoparticles were not clearly observable because they were coated tightly by antisera.


Figure 2
View larger version (11K):
[in this window]
[in a new window]
  		Figure 2. Graph of the reaction principle.

The filled circles represent gold particles, the branched lines and the stars represent antibody and antigen, respectively. The straight lines represent PEG.

immunoresonance scattering assay procedure
PB solution (0.50 mL of pH 6.4 solution for ApoAI or 0.30 mL of pH 6.2 solution for ApoB), gold-labeled antisera (1.2 mL of 58 mg/L gold-labeled ApoAI antisera or 1.2 mL of 58 mg/L gold-labeled ApoB antisera), a certain quantity of ApoAI (or ApoB), and 0.45 mL of 500 g/L PEG-6000 were successively added to 10-mL graduated tubes. The mixed solutions were diluted to 3.0 mL with distilled water, mixed well, and then deposited in an ultrasonic reactor (59 KHz) for 15 min at 37 °C. Suitable volumes of the prepared solutions were transferred to a quartz cell. The low sensitive file setting and a longitudinal coordinate scale of 6 were chosen, and the synchronous scattering spectrum of the system was recorded by means of synchronous scanning of excitation wavelength ({lambda}ex) and emission wavelength ({lambda}ex; {lambda}ex – {lambda}em = {Delta}{lambda} = 0) on the Model RF-540 spectrofluorophotometer. The RS intensity (IRS) at 560 nm was then recorded. The IRS values of blank solutions with no ApoAI or ApoB [(IRS)b] were also measured. The values for {Delta}I = IRS – (IRS)b were calculated.


   Results and Discussion
Top
 Abstract
 Introduction
 Materials and Methods
 Results and Discussion
References
 
The gold nanoparticles were found opposite to the globular heads at the N-terminal ends of the heavy chains of the antibodies (26). In the absence of PEG, gold-labeled ApoAI and ApoB antisera can combine with ApoAI and ApoB, respectively, to form gold-labeled immunocomplexes (ICs). The resulting RS intensity is very weak, however. Results indicate that the gold particle is not released from the IC and that the gold nanoparticles do not aggregate to form larger particles. In the presence of PEG, the labeled gold nanoparticles were liberated from the antisera and aggregated to form large particles (Fig. 1Up ), with the immune reaction continuing. Because of the correlation of RS intensity with the size of the gold particles(22)(23), the intensity was greatly enhanced. The process is shown in Fig. 2Up . The RS intensity increased linearly with ApoAI and ApoB concentration.

rs spectrum
ApoAI and ApoB are water-soluble macromolecular hydrophilic colloidal proteins with weak synchronous scattering. There are 2 resonance-scattering peaks, at 340 and 400 nm, and a synchronous scattering peak at 470 nm, where the apparatus has the strongest emission (27). After idiosyncratic reactions take place between the apolipoproteins and their respective antisera, the IC forms and aggregates to a certain degree because of its hydrophobic properties, enhancing the RS intensities. The strongest RS peaks of the IC are at 340 and 520 nm. Colloidal gold exhibits 3 RS peaks, at 320, 390, and 560 nm, and an apparatus self-producing synchronous scattering peak at 470 nm(24). Among those peaks, the peak intensity at 560 nm is the strongest(24). The small size of the gold nanoparticles used to label the antisera led to weak RS intensities for ApoAI (see Fig. 3 ) and ApoB (see Fig. 3 in the online Data Supplement). Immune reactions between the apolipoproteins and their respective antisera led to IC formation, release of colloidal gold from the antisera, and aggregation through the action of PEG. Intensities increased linearly with ApoA1and ApoB concentrations.


Figure 3
View larger version (15K):
[in this window]
[in a new window]
  		Figure 3. RS spectrum of gold-labeled goat anti-human ApoAI antiserum and ApoAI.

Traces: (a), PB solution (pH 6.4) containing 23.18 mg/L goat anti-human ApoAI antiserum and 75 g/L PEG-6000; (b), PB solution (pH 6.4) containing 23.18 mg/L goat anti-human ApoAI antiserum, 0.033 mg/L ApoAI, and 75 g/L PEG-6000; (c), PB solution (pH 6.4) containing 23.18 mg/L goat anti-human ApoAI antiserum, 0.17 mg/L ApoAI, and 75 g/L PEG-6000; (d), PB solution (pH 6.4) containing 23.18 mg/L goat anti-human ApoAI antiserum, 0.33 mg/L ApoAI, and 75 g/L PEG-6000.

selection of the PH, type, and volume of buffer solution
We tested the influence of PB solution (pH 5.8–8.0) and Tris-HCl (pH 7.0–8.5) buffer solution on the {Delta}IRS. PB solution had a positive effect on the system and was chosen for use. The maximum {Delta}IRS occurred in PB solution at pH 6.4 for ApoAI and PB solution at pH 6.0 for ApoB. As a result of tests of buffer solution concentration, we chose 0.030 mol/L PB solution for ApoAI and 0.020 mol/L PB solution for ApoB.

effect of gold-labeled APOAI and APOB antiserum concentrations
We investigated the influence on {Delta}IRS of different concentrations of gold-labeled antisera. In a certain range of concentrations, with the increase in gold-labeled antisera, the value of {Delta}IRS increased. The maximum {Delta}IRS values for both assays were attained at a gold-labeled antiserum concentration of 23.2 mg/L.

effect of peg concentration
PEG can bring about the aggregation of the IC, causing the release of gold particles. This aggregation is reversible, and the deposited proteins have no effect on bioactivity (28). Our results demonstrated that {Delta}IRS values increased greatly with increased PEG concentrations (see Figs. 4 and 5 in the online Data Supplement) owing to gold nanoparticle aggregation. Maximum {Delta}IRS values for the ApoAI and ApoB systems occurred at a PEG-6000 concentration of 75 g/L.


Figure 4
View larger version (14K):
[in this window]
[in a new window]
  		Figure 4. Linear regression analysis for ApoAI


Figure 5
View larger version (17K):
[in this window]
[in a new window]
  		Figure 5. Linear regression analysis for ApoB

effect of ultrasonic irradiation incubation time
We tested the influence of ultrasonic irradiation incubation time from 0 to 40 min on the IRS values of the ApoAI and ApoB systems. Under the conditions of ultrasonic irradiation at 37 °C, when the ApoAI (or ApoB) concentration was higher, the incubation was quicker, and incubation was slower when the ApoAI (or ApoB) concentration was lower. When the incubation lasted 15 min, all reactions ran to completion and the experimental results were stable. We therefore chose ultrasonic irradiation at 37 °C for 15 min for the 2 systems. The results of the experiment indicate that the {Delta}I was slower when PEG-6000 was added after the incubation of gold-labeled antibody and antigen than when PEG-6000 was added immediately before the incubation.

linear range
Using solutions with different concentrations, we tested the relationship between ApoAI and ApoB concentrations (x) and their corresponding intensities ({Delta}I; y). The linear range for ApoAI was 0.00833–0.3333 mg/L, the linear regression equation was {Delta}I = 180.5x + 5.96, the correlation coefficient was 0.9978, and the detection limit was 2.04 µg/L; for ApoB, the linear range was 0.00197 – 0.1972 mg/L, the regression equation was {Delta}I = 579.6x – 0.96, the correlation coefficient was 0.9988, and the detection limit was 0.96 µg/L. The IRS values were 77.4 for ApoAI at 0.3333 mg/L and 123.1 for ApoB at 0.1972 mg/L.

effects of interfering substances
We tested the effects of potentially interfering substances on the measurement of ApoAI and ApoB. When ApoAI and ApoB concentrations were 60.0 mg/L with relative error of ± 8%, the examined substances did not significantly interfere with the analysis (Table 1 ).


View this table:
[in this window]
[in a new window]
  		Table 1. Selectivity of the assay (0.06 mg/L ApoB).

comparison study
We analyzed 25 serum samples obtained from apparently healthy men at No. 5 Hospital of Guilin City (Figs. 4Up and 5Up ; also see Tables 3 and 4 in the online Data Supplement). Their mean (SD) totals by this assay were 1263 (107.6) mg/L for ApoAI and 853.2 (81.9) mg/L for ApoB. The samples were also assayed by immunoturbidimetry (14). The linear regression analysis revealed a correlation coefficient, slope, and intercept of 0.915, 0.966, and 68.53 mg/L for ApoAI, and 0.919, 0.996, and 15.46 mg/L for ApoB, respectively. The results obtained with both methods were consistent with published reference intervals for serum(29).

In conclusion, using this novel approach we were able to determine the concentrations of ApoAI and ApoB.


   Acknowledgments
 
This work was supported by the National Natural Scientific Foundation of China (20365001) and the Guangxi Foundation of New Century Ten-Hundred-Thousand Talents.


   Footnotes
 
1 Nonstandard abbreviations: ApoAI, apolipoprotein AI; ApoB, apolipoprotein B; RS, resonance scattering; PB, phosphate-buffered; PEG, polyethylene glycol; and IC, immunocomplex.


   References
Top
 Abstract
 Introduction
 Materials and Methods
 Results and Discussion
 References
 

  1. Steinberg KK, Cooper GR, Graiser SR. Some consideration of methodology and standardization of apolipoprotein A-I immunoassay. Clin Chem 1983;29:415-426.[Abstract/Free Full Text]
  2. Rosseneu M, Vercaemst R, Steinberg KK, Cooper GR. Some consideration of methodology and standardization of apolipoprotein B immunoassay. Clin Chem 1983;29:427-433.[Abstract/Free Full Text]
  3. Conotois JH, McNamara JR, Lammi-Keefe CJ. Reference interval for plasma apolipoprotein A-I determined with a standardized commercial immunoturbidimetric assay: results from Framingham Offspring Study. Clin Chem 1996;42:507-514.[Abstract/Free Full Text]
  4. Contois JH, McNamara JR, Lammi-Keefe CJ, Wilson PW, Massov T, Schaefer EJ. Reference interval for plasma apolipoprotein B determined with a standardized commercial immunoturbidimetric assay: results from Framingham Offspring Study. Clin Chem 1996;42:515-523.[Abstract/Free Full Text]
  5. Brown G, Albers JJ, Fisher LD. Regression of coronary artery disease as a result o intensive lipid-lowering therapy in men with high levels of apolipoprotein B. N Engl J Med 1984;311:1929-1932.
  6. Sniderman AD. Apolipoprotein B and apolipoprotein A1 as predictors of coronary artery disease. Can J Cardiaol 1988;4(Suppl A):24A-30A.
  7. Yla-Herttuala S, Palinski W, Rosenfcld ME. Lipoprotein in normal and atherosclerotic aorta. Eur Heart J 1990;11(Suppl E):88-99.
  8. Zago LB, Slobodianik NH, Gasali F, Torino F, Rio ME. Apolipoproteins A-I and B as predictors of complications in gallbladder lithiasis surgical patients. Nutrition 2003;19:250-252.[CrossRef][ISI][Medline] [Order article via Infotrieve]
  9. Pan XR, Hu SX, Gand H. Lipoprotein and apolipoprotein A1 levels in diabetics and coronary heart disease patients and controls. Chin Med J 1987;100:204-207.[Medline] [Order article via Infotrieve]
  10. Wang JJ. Rocket immunoelectrophoresis method for the content of serum apolipoprotein A1 and B. Shanghai Yixue Jianyan Zazhi 1986;1:26-28.
  11. He RX. Radioactivity immunoanalysis for serum apolipoprotein B. Chin J Nuclear Med 1986;6:85-88.
  12. Makoto K, Masaaki K, Teruhiko M, Tamio T. Determination of apolipoprotein B in serum by a sandwich ELISA. Clin Chim Acta 2005;351:115-120.[CrossRef][ISI][Medline] [Order article via Infotrieve]
  13. Hartmut ML, Rainer L, Angelika E, Weiler EG, Wolfgang V. Capillary electrophoresis, a rapid and sensitive method for routine analysis of apolipoprotein A-I in clinical samples. J Chromatogr A 1995;717:25-31.[CrossRef][ISI][Medline] [Order article via Infotrieve]
  14. Wang JJ, Li JZ. Light-scattering and light-transmission turbidimetric analysis for serum apolipoproteins A-I and B. Chin J Med Lab Sci 1988;11:2-7.
  15. Xi ZG. Application of Nanotechnique to Environment and Health 2004:24-40 Chemical Industry Press Beijing. .
  16. Pasternack PF, Bastamante C, Collings PJ, Gianncttd A, Giannetto Gibbs EJ. Resonance light scattering: a new technique for studying chromophore aggregation. J Am Chem Soc 1993;115:5393-5399.[CrossRef]
  17. Huang CZ'Li YF, Liu XD. Determination of nucleic acids at nanogram levels with safranine by a preresonance light-scattering technique. Anal Chim Acta 1998;375:89-97.[CrossRef]
  18. Huang CZ, Li YF, Shi YD, Shu RL. Assembly of methylene blue on nucleic acid template as studied by resonance light-scattering technique and determination of nucleic acids at nanogram levels. Bull Chem Soc Jpn 1999;72:1501-1508.[CrossRef]
  19. Liu S, Luo H, Li N, Liu Z, Zheng W. Resonance Rayleigh scattering study of the interaction of heparin with some basic diphenyl naphthylmethane dyes. Anal Chem 2001;73:3907-3914.[Medline] [Order article via Infotrieve]
  20. Luo HQ, Liu SP, Liu ZF, Liu Q, Li NB. Resonance Rayleigh scattering spectra for studying the interaction of heparin with some basic phenothiazine dyes and their analytical application. Anal Chim Acta 2001;449:261-270.[CrossRef]
  21. Jiang ZL, Pan HC, Yuan WE. Change color effect and spectral properties of gold nanoparticle-cationic surfactants system. Chem Res Chin Universities 2004;20:523-528.
  22. Zhu LP, Chen XQ. Common Experimental Method for Immunology 1999:426-430 People’s Military Medicine Press Beijing. .
  23. Jiang ZL, Feng ZW, Li TS, Li F, Zhong FX, Xie JY, et al. Resonance scattering spectroscopy of gold nanoparticle. Sci China B 2001;31:183-188.
  24. Pan HC, Jiang ZL, Yuan WE, Huang SY. Relationship between resonance scattering and resonance absorbance of gold nanoparticles. Chin J Appl Chem 2005;22:282-285.
  25. Chen X, Li T. Clinical Immunology and Immunology Techique 2002:44-46 People’s Military Medicine Press Beijing. .
  26. Steffen W. Immunogold localisation of the intermediate chain within the protein complex of cytoplasmic dynein. J Struct Biol 1996;117:227-235.[CrossRef][ISI][Medline] [Order article via Infotrieve]
  27. Jiang ZL. Nanoparticle and Resonance Scattering Spectroscopy 2003:90 Guangxi Normal University Press Guilin. .
  28. Wu JG. Application of Clinical Immunology Test [M] 1990:218-219 Jiangsu Scientific Technology Press Nanjing. .
  29. Li Y, Zhuang YY. Reference survey for serum apolipoprotein AI and B. J Clin Test 1999;16:333-337.



The following articles in journals at HighWire Press have cited this article:


Home page
 J Biomol ScreenHome page
Z. Jiang, L. Wei, M. Zou, A. Liang, and M. Meng
Rapid Assay of Trace Immunoglobulin M by a New Immunonanogold Resonance Scattering Spectral Probe
J Biomol Screen, April 1, 2008; 13(4): 302 - 308.
[Abstract] [PDF]

Home page
 Clin. Chem.Home page
Z. Jiang, W. Huang, J. Li, M. Li, A. Liang, S. Zhang, and B. Chen
Nanogold Catalysis Based Immunoresonance-Scattering Spectral Assay for Trace Complement Component 3
Clin. Chem., January 1, 2008; 54(1): 116 - 123.
[Abstract] [Full Text] [PDF]

This Article
Right arrow Abstract Freely available
Right arrow Full Text (PDF)
Right arrow 061176.Supplemental Data
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (20)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jiang, Z.
Right arrow Articles by Qin, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jiang, Z.
Right arrow Articles by Qin, A.
Related Collections
Right arrow Automation and Analytical Techniques

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS