Biomedical subjects

Dejiang Gao

Publications and source records attributed to Dejiang Gao.

6 recordsLinked to original sources

PubMed2006

Resonance light scattering technique for the determination of proteins with polymethacrylic acid (PMAA).

As a resonance light scattering (RLS) probe, the polyelectrolyte polymethacrylic acid (PMAA) was applied in this assay. The bovine serum albumin (BSA) and human serum albumin (HSA) were determined by the electrostatic interaction of PMAA and proteins. At pH 3.8 Na(2)HPO(4)-citric acid buffer solution, the RLS intensities of PMAA-BSA (HSA) system were greatly enhanced. The characteristic peaks were appeared at the wavelength 320, 546 and 594 nm. The optimization conditions of the reaction were also examined and selected. Under the selected conditions, the RLS intensities were proportional to the protein concentrations in the range of (0.0200-2.00) x 10(-6) mol/L for BSA and (0.0200-2.40) x 10(-6) mol/L for HSA. The influences of some foreign substances were also examined. The synthetic samples containing proteins and some real samples were analyzed and the results obtained were satisfactory.

Animals↗

PubMed2006

Determination of serum albumin in the presence of poly(diallyldimethylammonium chloride) by resonance light scattering technique.

By means of the resonance light scattering (RLS) technique, a new method was developed to determine the bovine serum albumin (BSA) and human serum albumin (HSA) by the interaction of serum albumin with poly(diallyldimethylammonium chloride) (PDDA). At Tris-NaOH buffer solution, the RLS intensity of serum albumin at the wavelength 320, 550 and 590 nm was obviously enhanced in the presence of PDDA. The influences of some experimental factors, including incubation time, addition sequence of reagents, pH value, concentration of PDDA and foreign substances, on the enhancement of the RLS intensity were examined. The optimum conditions of the experiment were selected. Under the selected experimental condition, the enhanced RLS intensities were directly proportional to the concentrations in the range of (0.0250-2.75)x10(-6) mol/L for BSA and (0.0235-1.17)x10(-6) mol/L for HSA. The detection limits (S/N=3) were 8.40x10(-9) mol/L for BSA and 7.39x10(-9) mol/L for HSA. The synthetic samples were analysed and the results obtained were satisfactory.

Animals↗

PubMed2006

Investigation on hyperin-cetyltrimethylammonium bromide-fibronectin system by resonance light-scattering technique.

A simple, highly sensitive assay for fibronectin (Fn) was reported using resonance light-scattering (RLS) technique based on the enhanced RLS intensity of hyperin-cetyltrimethylammonium bromide (CTMAB)-Fn system. The interaction system of hyperin-CTMAB-Fn was investigated using spectral methods. Mechanistic investigations show that the main reason of the enhanced RLS intensity of Fn is the formation of three-component complex (hyperin-CTMAB-Fn), in which CTMAB acts as a bridge between hyperin and Fn. The effects of pH, surfactant, concentration of CTMAB and hyperin, incubation time and foreign substances on the enhancement of RLS intensity were studied. Under the optimum conditions, the enhancement of RLS intensity is in proportion to the concentration of Fn in the range of 1.9-248ng/ml. The synthetic samples containing Fn were analyzed and results obtained were satisfied.

Cetrimonium↗

PubMed2006

Investigation on the interaction between colloidal gold and human complement factor 4 at different pH by spectral methods.

The interaction between colloidal gold and human complement factor 4 (human C4) at different pH was investigated by spectral methods, including absorption and resonance light-scattering spectrometry. According to the changes of color and absorption spectra of colloidal gold solution in presence of human C4, the interaction between colloidal gold and human C4 was quantitatively investigated using a semi-empirical "flocculation parameter". At the same time, the changes of resonance light-scattering spectra and transmission electron microscopy (TEM) images indicate that the aggregation of colloidal gold happens by electrostatic interaction in presence of human C4 in the pH range 5-6. However, the colloidal gold solution remains stable at pH >6 and pH <5 due to the repulsive electrostatic interaction between colloidal gold and human C4. The flocculation parameter is directly proportional to the concentration of human C4 in the range from 9.7 to 233.0 microgl(-1). In addition, the interactions between the colloidal gold and bovine serum albumin (BSA) as well as human serum albumin (HSA) were also investigated using the same methods. It was found that there was no aggregation of colloidal gold in presence of BSA and HSA in the pH range 5-6. However, when the pH of solution is 4, the aggregation of colloidal gold happens. Because BSA and HSA have different structure, the intensity of aggregation of colloidal gold in presence of BSA is greater than that in presence of HSA at pH 4.

Animals↗

PubMed2005

Determination of human complement factor C4 using resonance light-scattering technique with sodium dodecylbenzene sulphonate probe.

Based on the interaction between human complement factor C4 (human C4) and sodium dodecylbenzene sulphonate (SDBS) and the resonance light-scattering (RLS) technique, a highly sensitive assay for human C4 using resonance light-scattering technique was developed. At pH 2.8 Na2HPO4-citric acid buffer solution, the RLS intensities of SDBS system at 283, 503 and 600 nm were obviously enhanced in the presence of human C4. The effects of surfactant, pH, incubation time, concentration of SDBS and foreign substances on the enhanced RLS intensity of system were investigated. Under the optimum conditions, the enhanced RLS intensity is directly proportional to the concentration of human C4 in the range of (0.5-120)x10(-6)gl-1 and the linear regression equation was obtained with high correlation coefficient. This RLS technique was applied to the determination of human C4 in some synthetic samples with good recovery. Moreover, it was found that the electrostatic interaction is the main binding force between SDBS and human C4.

Benzenesulfonates↗

PubMed2005

Studies on the interaction of colloidal gold and serum albumins by spectral methods.

The interactions of colloidal gold and serum albumins, including bovine serum albumin (BSA) and human serum albumin (HSA), were studied by fluorescence and absorption spectrometry. Fluorescence quenching spectrometry was applied to study the interactions between colloidal gold and serum albumins. At pH 7.4 phosphate-buffered saline (PBS), the intensity of fluorescence emission spectrum of serum albumins decreased in the presence of colloidal gold, which indicated that colloidal gold quenched the fluorescence of serum albumins. Experimental results indicated that the combination reactions of colloidal gold and serum albumins were static quenching processes. Based on the effect of colloidal gold on fluorescence intensity, the binding constants, the numbers of binding sites and the acting forces between colloidal gold and serum albumins were found.

Animals↗