scholarly journals Corrigendum to “Development and Evaluation of an Immuno-Capture Enzyme-Linked Immunosorbent Assay to Quantify the Mycoplasma capricolum subsp. Capripneumoniae (Mccp) Protein in Contagious Caprine Pleuropneumonia (CCPP) Vaccine”

2021 ◽  
Vol 2021 ◽  
pp. 1-1
Author(s):  
Jean de Dieu Baziki ◽  
Charles Bodjo S. ◽  
Nick Nwankpa ◽  
Naomi Maina ◽  
Ethel Chitsungo ◽  
...  
Keyword(s):  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Mycoplasma Capricolum ◽  
Contagious Caprine Pleuropneumonia

scholarly journals Development and Evaluation of an Immuno-Capture Enzyme-Linked Immunosorbent Assay to Quantify the Mycoplasma capricolum subsp. capripneumoniae (Mccp) Protein in Contagious Caprine Pleuropneumonia (CCPP) Vaccine

2020 ◽  
Vol 2020 ◽  
pp. 1-10
Author(s):  
Jean de Dieu Baziki ◽  
Bodjo S. Charles ◽  
Nick Nwankpa ◽  
Naomi Maina ◽  
Ethel Chitsungo ◽  
...  
Keyword(s):  
Reference Sample ◽  
Current Method ◽  
Enzyme Linked Immunosorbent Assay ◽  
Internal Reference ◽  
Mycoplasma Capricolum ◽  
Contagious Caprine Pleuropneumonia ◽  
Effective Manner ◽  
Batch Release

An effective contagious caprine pleuropneumonia (CCPP) vaccine is essential for the increased production of healthy goats in a cost-effective manner and the prevention of animal-to-animal transmission for both domestic animals and wildlife. Quality control of this vaccine ensures that a reliable supply of pure, safe, and potent batches is obtained. As part of this control, in vitro quantification of Mycoplasma capricolum subsp. capripneumoniae (Mccp) protein in the final vaccines is required before the CCPP vaccine undergoes batch release and certification. The current method used for quantification is based on the measurement of total protein using the bicinchonic acid (BCA) test. This method quantifies the total amount of protein in the vaccine including contaminant protein from media, which can lead to overestimation of the quantity of Mccp protein, resulting in reduced vaccine immunogenicity. An immuno-capture ELISA (ICE) was developed for specific detection and quantification of the Mccp antigen in the CCPP vaccine. As the ICE detects and measures the amount of antigen between two layers of antibodies, capture and detecting antibodies are required. Mouse monoclonal antibodies (mAbs) that detect the Mccp antigen were produced and characterized. One of these mAbs, Mccp-25, was used to develop the ICE as an unlabelled capture antibody and horseradish peroxidase conjugated detecting antibody. The ICE was standardized and evaluated using an internal reference sample, experimental CCPP vaccines and commercial CCPP vaccines. A comparison between the polymerase chain reaction (PCR) and ICE showed good correlation between the two assays. Also, an in vitro ICE method correlated well with an in vivo sero-conversion in goats that were vaccinated with selected test vaccines. The sensitivity of the ICE was estimated at 30 ng/ml.

scholarly journals Demonstration of cross-reactive antigens in F38 and related mycoplasmas by enzyme-linked immunosorbent assay (ELISA) and immunoblotting

1985 ◽  
Vol 95 (1) ◽  
pp. 95-106 ◽  
Author(s):  
M. Kanyi Kibe ◽  
D. E. Bidwell ◽  
P. Turp ◽  
G. R. Smith
Keyword(s):  
Immunosorbent Assay ◽  
Immunoblot Analysis ◽  
Cross Reactivity ◽  
Mycoplasma Species ◽  
Enzyme Linked Immunosorbent Assay ◽  
Major Protein ◽  
Protein Antigens ◽  
Contagious Caprine Pleuropneumonia ◽  
Mycoplasma Mycoides ◽  
Immunoblotting Technique

SUMMARYThe ELISA and an immunoblotting technique were used to study F38-type mycoplasmas – an important cause of contagious caprine pleuropneumonia – and a number of related mycoplasma species, subspecies, types or serogroups.Two-way ELISA cross-reactivity was demonstrated between five mycoplasmas, namely strain F38,Mycoplasma mycoidessubsp.mycoides(LC strain),M. equigenilalium, M. primatumand bovine serogroup 7. In addition one-way cross-reactivity was demonstrated between F38 and each of the following mycoplasmas:M. mycoidessubsp.mycoides(two SC strains),M. mycoidessubsp.capri, and bovine serogroup L. F38 andM. capricolumdid not cross-react.Immunoblot analysis, unlike ELISA, revealed that F38 andM. capricolumwere closely related. At least four major protein antigens were shared between F38,M. mycoidessubsp.mycoides(SC and LC strains),M. mycoidessubsp.capriand bovine serogroup 7. The ELISA cross-reactions (above) shown byM. equigenitaliumandM. primatumwith each other, with F38 and with other mycoplasmas were not apparent by immunoblotting.

Plasminogen Interactions with Immobilized Fibrinogen

1989 ◽  
Vol 62 (04) ◽  
pp. 1078-1082 ◽  
Author(s):  
Burt Adelman ◽  
Patricia Ouynn
Keyword(s):  
Immunosorbent Assay ◽  
Aminocaproic Acid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Binding Regions ◽  
Dose Dependent Fashion ◽  
Epsilon Aminocaproic Acid ◽  
Dose Dependent

SummaryThis report describes the binding of plasminogen to fibrinogen adsorbed onto polystyrene wells. Binding was determined by enzyme linked immunosorbent assay. Both glu- and lys-plasminogen bound to immobilized fibrinogen in a dose-dependent fashion. However, more lys- than glu-plasminogen bound when equal concentrations of either were added to immobilized fibrinogen. Plasminogen binding was inhibited by epsilon aminocaproic acid indicating that binding was mediated via lysine-binding regions of plasminogen. Soluble fibrinogen added in excess of immobilized fibrinogen did not compete for plasminogen binding but fibrinogen fragments produced by plasmin digestion of fibrinogen did. Treatment of immobilized fibrinogen with thrombin caused a small but significant (p <0.01) increase in plasminogen binding. These studies demonstrate that immobilized fibrinogen binds both glu- and lys-plasminogen and that binding is mediated via lysine-binding regions. These interactions may facilitate plasminogen binding to fibrinogen adsorbed on to surfaces and to cells such as platelets which bind fibrinogen.

Alterations in Vascular Endothelial Cell-related Plasma Proteins In Thalassaemic Patients and their Correlation with Clinical Symptoms

1995 ◽  
Vol 74 (04) ◽  
pp. 1045-1049 ◽  
Author(s):  
P Butthep ◽  
A Bunyaratvej ◽  
Y Funahara ◽  
H Kitaguchi ◽  
S Fucharoen ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Immunosorbent Assay ◽  
Plasma Proteins ◽  
Clinical Symptoms ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial Cell ◽  
Enzyme Linked Immunosorbent Assay ◽  
Vascular Endothelial ◽  
Leg Ulcers

SummaryAn increased level of plasma thrombomodulin (TM) in α- and β- thalassaemia was demonstrated using an enzyme-linked immunosorbent assay (ELISA). Nonsplenectomized patients with β-thalassaemia/ haemoglobin E (BE) had higher levels of TM than splenectomized cases (BE-S). Patients with leg ulcers (BE-LU) were found to have the highest increase in TM level. Appearance of larger platelets in all types of thalassaemic blood was observed indicating an increase in the number of younger platelets. These data indicate that injury of vascular endothelial cells is present in thalassaemic patients.

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