Study on the fluorescence properties of the interaction between felodipine and bovine serum protein

The interaction between felodipine and bovine serum protein was studied, the optimal experimental conditions were selected, and the fluorescence quenching mechanism was discussed. The interaction between filodipine and bovine serum protein was determined by UV spectrophotometry, and the optimal experimental conditions were selected by control variable method. The mechanism of fluorescence quenching in the system was explored by fluorescence spectrophotometry. The fluorescence intensity of the system between felodipine and bovine serum protein was the most obvious under the experimental conditions of buffer solution pH 7.4, felodipine concentration 8.0*10-4mol/L, reaction time 30min and 25°C. Static fluorescence quenching caused by the formation of complex compounds.

Evaluation of usefulness of a commercial agarose gel electrophoresis kit (QuickGel SP) for bovine serum protein electrophoresis

The aim of this study was to show the usefulness of a commercial agarose gel electrophoresis (AGE) kit (QuickGel SP) for separating bovine serum protein fractions in comparison with conventional cellulose acetate electrophoresis (CAE). Serum protein bands were verified using five reference reagents corresponding to albumin and α1-, β1-, β2-, and γ-globulins. AGE clearly revealed six separated fractions of albumin and α1-, α2-, β1-, β2-, and γ-globulin fractions in 100% and 77.8% in serum samples of dairy cows from the healthy (n=27) and diseased groups (n=27), respectively. The α1- and α2-globulins were not separated by CAE in 14.8% and 96.3% of the samples from the healthy and diseased groups, respectively, whereas β2- and γ-globulin were not separated by CAE in 96.3% and 100% of the samples from the healthy and diseased groups, respectively. More than 94% of the points for the α-globulin fractions (α1- and α2-globulins), the β-γ-globulin fractions (β1-, β2-, and γ-globulins), and the albumin/globulin ratio between AGE and CAE were within agreement on the Bland-Altman plots. However, the mean biases were not near zero in the albumin and β-γ-globulin fractions. These results suggest that the high-resolution commercial AGE kit can be utilized to separate bovine serum protein fractions.

An on–off–on gold nanocluster-based fluorescent probe for sensitive detection of organophosphorus pesticides

In this study, a highly sensitive fluorescent probe based on bovine serum protein-protected gold nanoclusters (BSA-AuNCs) was developed for the determination of organophosphorus pesticides (OPs).

Study on the Quality of Lyophilized Human Diploid Cell Rabies Vaccine Using Microcarrier Technology

<p>The aim is to study the potency, purity, safety, and stability of the lyophilized human diploid cell rabies vaccine (HDCV). The viruses were harvested from infected human diploid cells (MRC-5 strain) which were cultured in a microcarrier bioreactor. After harvest, purification, inactivation and lyophilization, HDCV was produced. The potency of vaccines was measured by NIH method; the bovine serum protein residual content and the antibiotic residues were tested by ELISA method; the endotoxin content was detected by semi quantitative gel method; the safety of vaccine was determined <em>in vivo</em>. Among 6 batches of HDCV, the lowest immunizing potency was 4.79 IU/ml, whilst the highest was 6.03 IU/ml; the lowest bovine serum protein residual content was 12.41 ng/dose, whilst the highest was 31.74 ng/Dose; the content of antibiotic residues was from 2.20 ng/ml to 4.00 ng/ml; endotoxin levels were all lower than 50 EU/dose. All the mice and guinea pigs vaccinated were all alive, and the body weight of each mouse also increased. The stability was investigated by determining the water content and potency of the vaccine placed in 37±1 °C for 4 weeks and 2-8 °C for 48 months, respectively. The results indicate all the quality index accords with the standards of “Pharmacopoeia of the People's Republic of China 2010, 3 Volumes”. HDCV shows satisfactory potency, purity, safety, and stability.</p>