The effect of chlorophyll on the enzyme‐linked immunosorbent assay ( ELISA ) of procymidone in vegetables and the way to overcome the matrix interference

2021 ◽  
Author(s):  
Ziang Zhang ◽  
Hong Lin ◽  
Jianxin Sui ◽  
Xiangning Han ◽  
Luefeng Wang ◽  
...  
Keyword(s):  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Matrix Interference ◽  
The Matrix ◽  
The Way

Sensitive Streptavidin-Biotin Enzyme-Linked Immunosorbent Assay for Rapid Screening of Chloramphenicol Residues in Swine Muscle Tissue

1990 ◽  
Vol 73 (4) ◽  
pp. 534-540
Author(s):  
Cornelis Van De Water ◽  
Nel Haagsma
Keyword(s):  
Muscle Tissue ◽  
Immunosorbent Assay ◽  
Sample Solution ◽  
Rapid Screening ◽  
Enzyme Linked Immunosorbent Assay ◽  
Aqueous Sample ◽  
Response Curves ◽  
Antibody Preparation ◽  
Muscle Tissues ◽  
The Matrix

Abstract A sensitive, competitive enzyme-linked Immunosorbent assay (ELISA) for chloramphenicol (CAP) in swine muscle tissue has been developed. The ELISA Is based on an earlier procedure. To Improve sensitivity, different optimization procedures were Investigated. The introduction of a streptavldln- biotln system and the use of a coating antigen with a lower CAP Incorporation resulted In the most sensitive ELISA: the CAP concentration giving 50% Inhibition decreased from 125 ng/mL to 3.0 ng/mL. This ELISA procedure was applied for a rapid screening of CAP residues In swine muscle tissue. The tissues were extracted with demlneral- Ized water. A concentrated phosphate-buffered saline solution was added to the filtered aqueous extract and this sample solution was directly submitted to the ELISA procedure. The results were compared to values obtained by analysis of a corresponding blank. This blank was prepared by treating a part of the aqueous sample solution with an immobilized monoclonal antibody preparation. This treatment was necessary because aqueous extracts of different swine muscle tissues showed a high variation In dose-response curves, probably caused by the complexity and variability of the matrix. In spiked tissues, the presence of CAP at concentrations of 10 μg/kg and higher can be easily demonstrated.

scholarly journals Rapid Determination of Ractopamine Residues in Edible Animal Products by Enzyme-Linked Immunosorbent Assay: Development and Investigation of Matrix Effects

2009 ◽  
Vol 2009 ◽  
pp. 1-9 ◽  
Author(s):  
Yan Zhang ◽  
FengXia Wang ◽  
Li Fang ◽  
Shuo Wang ◽  
GuoZhen Fang
Keyword(s):  
Immunosorbent Assay ◽  
Matrix Effects ◽  
Limit Of Detection ◽  
Rapid Determination ◽  
High Sensitivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Liver Sample ◽  
Pig Liver ◽  
Animal Products ◽  
The Matrix

To determine ractopamine residues in animal food products (chicken muscle, pettitoes, pig muscle, and pig liver), we established a rapid direct competitive enzyme-linked immunosorbent assay (ELISA) using a polyclonal antibody generated from ractopamine-linker-BSA. The antibody showed high sensitivity and specificity in phosphate buffer, with anIC50of 0.6 ng/mL, and the limit of detection was 0.04 ng/mL. The matrix effect of the samples was easily eliminated by one-step extraction with PBS, without any organic solution or clean-up procedure such as SPE or liquid-liquid extraction, making it a much more simple and rapid method than previously reported ones. The detection limit in blank samples was 0.2 μg/kg. To validate this new RAC (ractopamine hydrochloride) ELISA, a RAC-free pig liver sample spiked at three different concentrations was prepared and analyzed by HPLC and ELISA. The results showed a good correlation between the data of ELISA and HPLC (R2>0.95), which proves that the established ELISA is accurate enough to quantify the residue of RAC in the animal derived foods.

Enzyme-Linked Immunosorbent Assay for the Determination of Five Organophosphorus Pesticides in Camellia Oil

2014 ◽  
Vol 77 (7) ◽  
pp. 1178-1183 ◽  
Author(s):  
YIHUA LIU ◽  
YIRONG GUO ◽  
GUONIAN ZHU ◽  
FUBIN TANG
Keyword(s):  
Immunosorbent Assay ◽  
Solid Phase ◽  
Organophosphorus Pesticides ◽  
Enzyme Linked Immunosorbent Assay ◽  
Regulatory Requirements ◽  
Camellia Oil ◽  
The Matrix ◽  
Interassay Coefficient ◽  
Assay Conditions

A matrix solid-phase dispersion and direct competitive enzyme-linked immunosorbent assay (MSPD-ELISA) was developed for five organophosphorus pesticides (OPs) in camellia oil. Seven haptens with different substituents in the aromatic ring were used to prepare different competitors; the ELISA showed highest sensitivity and specificity to OPs when the competitor had moderate heterology to the immunizing hapten. Several assay conditions were optimized to increase the ELISA sensitivity. The optimized ELISA for five OPs had 50% inhibitory concentrations of 6.3 ng/ml (parathion), 18.9 ng/ml (methyl parathion), 120.7 ng/ml (fenitrothion), 110.4 ng/ml (fenthion), and 20.7 ng/ml (phoxim). The average recoveries of five OPs in camellia oil ranged from 75.7 to 105.3%, with the interassay coefficient of variations ranging from 6.0 to 13.4%. Compared with the results previously reported, the ELISA that was developed in the present study showed a much higher sensitivity. Additionally, MSPD was used in the sample preparation to minimize the matrix effect. Recoveries from the method developed here were in agreement with those obtained by gas chromatography, which indicated that the detection performance of the MSPD-ELISA could meet the regulatory requirements of different governments and international organizations.

scholarly journals Development of a Highly Sensitive and Specific Enzyme-Linked Immunosorbent Assay Based on Recombinant Matrix Protein for Detection of Avian Pneumovirus Antibodies

2000 ◽  
Vol 38 (11) ◽  
pp. 4010-4014 ◽  
Author(s):  
Baldev R. Gulati ◽  
Kjerstin T. Cameron ◽  
Bruce S. Seal ◽  
Sagar M. Goyal ◽  
David A. Halvorson ◽  
...  
Keyword(s):  
Immunosorbent Assay ◽  
Matrix Protein ◽  
Clinical Signs ◽  
M Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Serum Samples ◽  
Specific Test ◽  
Avian Pneumovirus ◽  
Highly Sensitive ◽  
The Matrix

The matrix (M) protein of avian pneumovirus (APV) was evaluated for its antigenicity and reliability in an enzyme-linked immunosorbent assay (ELISA) for diagnosis of APV infection, a newly emergent disease of turkeys in United States. Sera from APV-infected turkeys consistently contained antibodies to a 30-kDa protein (M protein). An ELISA based on recombinant M protein generated in Escherichia coli was compared with the routine APV ELISA that utilizes inactivated virus as antigen. Of 34 experimentally infected turkeys, 33 (97.1%) were positive by M protein ELISA whereas only 18 (52.9%) were positive by routine APV ELISA 28 days after infection. None of the serum samples from 41 uninfected experimental turkeys were positive by M protein ELISA. Of 184 field sera from turkey flocks suspected of having APV infection, 133 (72.3%) were positive by M protein ELISA whereas only 99 (53.8%) were positive by routine APV ELISA. Twelve serum samples, which were negative by M protein ELISA but positive by routine APV ELISA, were not reactive with either recombinant M protein or denatured purified APV proteins by Western analysis. This indicates that the samples had given false-positive results by routine APV ELISA. The M protein ELISA was over six times more sensitive than virus isolation (11.5%) in detecting infections from samples obtained from birds showing clinical signs of APV infection. Taken together, these results show that ELISA based on recombinant M protein is a highly sensitive and specific test for detecting antibodies to APV.

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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