38 research outputs found
Gestión de alarmas, usuarios y programación de calendarios
Novajarque Delicado, H. (2011). Gestión de alarmas, usuarios y programación de calendarios. https://riunet.upv.es/handle/10251/13283.Archivo delegad
Association between the anti-PA antibodies and state.
Box plots for the distribution of anti-PA antibodies. (A) Herds 1–8 in the endemic area and 9–12 in the nonendemic area. (B) Vaccination timing. The boxes indicate the interquartile range, the horizontal lines indicate the median, and the lower and upper hinges indicate the minimum and maximum values, respectively (outliers not included). Horizontal dotted line: cut-off value of 0.67.</p
Optimization of rPA-D1 ELISA.
(A) By using the checkerboard titrations, we determined the optimal concentrations of the antigen, the antibody and serum dilutions as follows: antigen, 10 ng/well; serum dilution, 1:100; second antibody dilution, 1:12,000. (B) Analysis of control serum samples using rPA-D1 ELISA under optimal conditions. NC: negative control group, (n = 53). PC: positive control group (n = 25). Red dot: pooled sample from cattle with exposure to natural infection. Error bars represent the mean and standard deviation. Horizontal dotted line: cut-off value of 0.67.</p
Production and purification of rPA-D1.
(A) Cartoon of full-length PA revealing the PA-D1 gene used in antigen preparation. (B) Western blot analysis of the affinity purification and desalting process: lane 1, total cell lysate; lane 2, pellet fraction; lane 3, supernatant fraction (PA-D1-GST: 54 kDa); lane 4, beads bound; lane 5, elute after treatment with PreScission Protease (PA-D1: 28 kDa); lane 6, desalting fraction. (C and D) Coomassie brilliant blue staining and Western blot analysis of the fractions collected during the cation exchange process. Lane 1, molecular weight marker; lane 2, sample loaded onto the cation exchange chromatography column; lane 3, flow through; lane 4, Resource-S fraction. Mw; molecular weight marker (in kDa), *: truncated product.</p
Proportion of seropositive cattle in the herds sampled.
Proportion of seropositive cattle in the herds sampled.</p
Sampling areas in the Western Province, Zambia.
The blood samples used in this study were collected from eight herds of cattle in the Nalolo District and Luampa Districts.</p
Horses anti-PAD1 immunoglobulin G (IgG) responses against subcutaneously injected <i>Bacillus anthracis</i> Sterne 34F2 strain spore vaccine.
(A) anti-PAD1 IgG response of vaccinated horses in serum dilution 1:100. Each serum sample was tested in technical triplicate by PAD1-ELISA. Checkerboard titration between PAD1 and (B) horse hyperimmunized anti-B. anthracis serum (PC1) or (C) naive horse serum (NC1) in PAD1-ELISA. Each dilution of serum sample was tested in technical triplicate. The twofold serum dilution starts with a dilution of 1:100, and PAD1 dilution starts with 1.6 μg/well. From the result, we determined the optimal concentrations of the antigen, antibody, and serum dilutions as follows: antigen, 0.4 μg/well; serum dilution, 1:100; second antibody dilution, 1:15,000.</p
Expression of CapA322.
(A and B) Coomassie brilliant blue staining (CBB) and Western blotting of proteins in cell lysate (lanes 2–5), supernatant (lanes 6–9), and pellet (lanes 10–13) fractions of control and CapA322 expressing Escherichia coli BTZ006 grown in terrific broth with or without isopropyl β-D-thiogalactopyranoside (IPTG) at 37°C for 4 h at 180 rpm. In Western blotting, the proteins were probed with anti-glutathione S-transferase (GST) immunoglobulin G. Lanes 1 and 14, Mw, molecular weight marker (in kDa). Control, E. coli BL21 harboring empty pGEX-6P-2 plasmid expressing GST (GST: 26 kDa). BTZ006, E. coli expressing recombinant CapA322 (GST-CapA322: 37 kDa). +, 0.2 mM IPTG induction; −, without IPTG induction. (TIF)</p
<i>In silico</i> selected CDSs for identification of immunoreactivity.
In silico selected CDSs for identification of immunoreactivity.</p
