Evidence for heterogeneity in the 160/165 × 10(3) Mr glycoprotein components of desmosomes

1987 ◽  
Vol 88 (4) ◽  
pp. 513-520
Author(s):  
J.C. Jones ◽  
K.L. Vikstrom ◽  
R.D. Goldman
Keyword(s):  
Monoclonal Antibodies ◽  
Polyclonal Antibody ◽  
Polyclonal Antibodies ◽  
Mouse Skin ◽  
Basal Cells ◽  
Antibody Preparation ◽  
Plaque Component ◽  
Mouse Tissues ◽  
Double Label ◽  
Cryostat Sections

We have prepared both monoclonal and polyclonal antibody preparations directed against the 160/165 × 10(3) Mr glycoproteins (desmogleins) of bovine tongue epithelial desmosomes. The polyclonal antibody preparation recognizes desmosomes in a number of mouse tissues, e.g. mouse skin, heart, bladder and trachea, as determined by immunofluorescence microscopy. Furthermore, the polyclonal antibodies recognize polypeptide(s), present in the high salt, Triton-insoluble residues (‘cytoskeleton preparations’) of mouse skin, heart, bladder and trachea, which comigrate with the 160/165 × 10(3) Mr glycoproteins of bovine tongue epithelial desmosomes as determined by ‘Western’ immunoblotting. Conversely, the monoclonal 160/165 × 10(3) Mr antibody preparation recognizes desmosomes of stratified squamous epithelial tissues but not desmosomes in other tissue types. Moreover, whereas the monoclonal antibodies recognize 160/165 × 10(3) Mr polypeptides in mouse skin cell cytoskeletons they show no immunoreactivity with the cytoskeleton preparations of mouse bladder, trachea and heart following immunoblotting. These results suggest therefore that although there are conserved epitopes of the 160/165 × 10(3) Mr glycoproteins there are also epitopes of these molecules which vary from tissue to tissue. Double label immunofluorescence observations of cryostat sections of mouse skin using the monoclonal antibodies and antibodies directed against desmoplakin, a plaque component of desmosomes, reveal that the monoclonal antibodies do not recognize certain desmosomes in basal cells which are recognized by desmoplakin antibodies. Indeed, double label observations of cryostat sections of mouse skin using the monoclonal antibodies and human autoantibodies which react with hemidesmosomal components suggest that the monoclonal antibodies stain desmosomes located along the apical surfaces of basal cells but fail to recognize desmosomes along the lateral surfaces of these same cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Differences in the exposure of C- and N-terminal tubulin domains in cytoplasmic microtubules detected with domain-specific monoclonal antibodies

1989 ◽  
Vol 92 (3) ◽  
pp. 519-528 ◽  
Author(s):  
P. Draber ◽  
E. Draberova ◽  
I. Linhartova ◽  
V. Viklicky
Keyword(s):  
Monoclonal Antibodies ◽  
Polyclonal Antibodies ◽  
Limited Proteolysis ◽  
Antigenic Determinants ◽  
Alpha Tubulin ◽  
Domain Specific ◽  
Double Label ◽  
Cytoplasmic Microtubules ◽  
C And N ◽  
Terminal Domains

A panel of 11 monoclonal antibodies specific to alpha- or beta-tubulin subunits was used to study the location of tubulin molecules in cytoplasmic microtubules. Specificity of antibodies was confirmed by immunoblotting and immunofluorescence experiments on fixed cells. The limited proteolysis of tubulin with trypsin and chymotrypsin followed by immunoblotting demonstrated that the antibodies discriminated between structural domains of both subunits. Epitope mapping of isolated alpha-tubulin revealed that a set of antibodies against the N-terminal domain of the alpha-subunit (TU-01, TU-02, TU-03, TU-09, 6–11B-1) recognized at least four different antigenic determinants. Immunofluorescence staining of unfixed detergent-extracted cells showed that antibodies to determinants on C-terminal domains labelled microtubules, but these were not decorated with antibodies to N-terminal domains. The same results were obtained after microinjection of antibodies into living cells. The unchanged distribution of microtubules in injected cells was confirmed by double-label immunofluorescence with polyclonal antibodies. The data indicate that while parts of C-terminal domains of both subunits are exposed on the exterior of the microtubules, considerable regions of the N-terminal domains are either not exposed on the surface of cytoplasmic microtubules, or are masked by interacting proteins.

scholarly journals Humans surviving cholera develop antibodies against Vibrio cholerae O-specific polysaccharide that inhibit pathogen motility

2020 ◽  
Author(s):  
Richelle C. Charles ◽  
Meagan Kelly ◽  
Jenny M. Tam ◽  
Aklima Akter ◽  
Motaher Hossain ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Vibrio Cholerae ◽  
Polyclonal Antibody ◽  
High Speed ◽  
Polyclonal Antibodies ◽  
Intestinal Lumen ◽  
Dependent Manner ◽  
Specific Antibodies ◽  
Specific Polysaccharide

ABSTRACTThe mechanism of protection against cholera afforded by previous illness or vaccination is currently unknown. We have recently shown that antibodies targeting O-specific polysaccharide (OSP) of Vibrio cholerae correlate highly with protection against cholera. V. cholerae is highly motile and possesses a flagellum sheathed in O-specific polysaccharide (OSP), and motility of V. cholerae correlates with virulence. Using high speed video microscopy, and building upon previous animal-related work, we demonstrate that sera, polyclonal antibody fractions, and OSP-specific monoclonal antibodies recovered from humans surviving cholera block V. cholerae motility at both subagglutinating and agglutinating concentrations. This anti-motility effect is reversed by pre-adsorbing sera and polyclonal antibody fractions with purified OSP; and is associated with OSP-specific but not flagellin-specific monoclonal antibodies. F[ab] fragments of OSP-specific polyclonal antibodies do not inhibit motility, suggesting a requirement for antibody-mediated crosslinking in motility inhibition. We show that OSP-specific antibodies do not directly affect V. cholerae viability, but that OSP-specific monoclonal antibody highly protects against death in the murine cholera model. We used in vivo competitive index studies to demonstrate that OSP-specific antibodies impede colonization and survival of V. cholerae in intestinal tissues, and that this impact is motility-dependent. Our findings suggest that the impedance of motility by antibodies targeting V. cholerae OSP contributes to protection against cholera.IMPORTANCECholera is a severe dehydrating illness of humans caused by Vibrio cholerae. V. cholerae is a highly motile bacterium that has a single flagellum covered in lipopolysaccharide (LPS) displaying O-specific polysaccharide (OSP), and V. cholerae motility correlates with its ability to cause disease. The mechanisms of protection against cholera are not well understood; however, since V. cholerae is a non-invasive intestinal pathogen, it is likely that antibodies that bind the pathogen or its products in the intestinal lumen contribute to protection from infection. Here, we demonstrate that OSP-specific antibodies isolated from humans surviving cholera in Bangladesh inhibit V. cholerae motility and are associated with protection against challenge in a motility-dependent manner.

Development of a Sandwich ELISA to Detect Hepcidin in Human Serum.

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 2000-2000 ◽  
Author(s):  
Tara L Arvedson ◽  
George Doellgast ◽  
Hossein Salimi-Moosavi ◽  
Chadwick King ◽  
Ian Foltz ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Polyclonal Antibody ◽  
Limit Of Detection ◽  
Sandwich Elisa ◽  
Alkaline Treatment ◽  
Detection Range ◽  
Antibody Preparation ◽  
Amino Acid Peptide ◽  
Class 1

Abstract Abstract 2000 Poster Board I-1022 Hepcidin is a 25 amino acid peptide that is the central mediator of iron metabolism. Iron excess, deficiency and maldistribution have been implicated in the etiology of many diseases including atherosclerosis, diabetes, neurodegeneration and the anemia of inflammation. Determination of hepcidin levels may be useful in diagnosis and treatment decisions for some or all of these diseases. Serum hepcidin measurement has so far been limited to a prohepcidin (60 amino acid hepcidin precursor) ELISA, mass spectrometry (MS)-based assays or competition ELISAs using polyclonal anti-hepcidin antibodies. The current work describes the generation of a sandwich ELISA using monoclonal antibodies to detect human hepcidin (hHepc) and optimization of assay conditions to resolve inconsistencies between MS- and ELISA-based detection. The ability of two anti-hHepc antibodies to sandwich (bind simultaneously) with hHepc was demonstrated using a rabbit polyclonal antibody preparation from hHepc-immunized animals. The same polyclonal antibody preparation was used for both hHepc capture and detection. The limit of detection achieved with this assay was O.D.450<1, suggesting that only a small proportion of the total antibodies could bind concurrently. To improve hHepc detection, a panel of monoclonal antibodies was screened for the ability to sandwich. Antibody epitope characterization studies using purified antibodies and >1000 hybridoma supernatants identified three classes of antibodies: classes 1 and 2 each recognized epitopes found in both full length mature hHepc (hHepc 25) and a shorter version (hHepc 20); class 3 bound a different epitope and demonstrated an increased affinity for hHepc 25 over hHepc 20. The majority of antibodies characterized were in class 1 while antibodies in classes 2 and 3 were rare (∼1% of antibody panel) highlighting the difficulty in achieving a sandwiching event. Antibodies 19D12 (class 1) and 23F11 (class 2) were identified as the optimal sandwich pair with a detection range of approximately 0.2-1000 ng/ml using synthetic hHepc. Initial comparisons of data generated using the sandwich ELISA and a fully-quantitative MS-based assay demonstrated a lack of consistent agreement. This issue was somewhat addressed by introduction of an alkaline treatment step to dissociate any protein/hHepc complexes in serum. Subsequent comparison of the two assays using sera from several different patient populations (anemia of cancer, chemotherapy-induced anemia, kidney disease) as well as healthy donors demonstrated good correlation (R2 range = 0.83-0.92; n=237). This sandwich ELISA may represent a tool for aligning the MS and ELISA-generated results in a format that has the potential to be high throughput and widely available. Disclosures: Arvedson: Amgen: Employment. Doellgast:Amgen: Employment. Salimi-Moosavi:Amgen: Employment. King:Amgen: Employment. Foltz:Amgen: Employment. Chen:Amgen: Employment. Li:Amgen: Employment. Sasu:Amgen: Employment.

scholarly journals Cross-reactivity of antibodies specific for flagellar tektin and intermediate filament subunits.

1987 ◽  
Vol 104 (6) ◽  
pp. 1563-1568 ◽  
Author(s):  
X J Chang ◽  
G Piperno
Keyword(s):  
Monoclonal Antibodies ◽  
Intermediate Filament ◽  
Immunofluorescence Microscopy ◽  
Polyclonal Antibodies ◽  
Nuclear Lamina ◽  
Helical Structure ◽  
Cross Reactivity ◽  
Cytoskeletal Proteins ◽  
Intermediate Filament Proteins ◽  
Double Label

Monoclonal antibodies specific for each of the flagellar tektins were prepared and used to determine whether structures similar to tektin filaments are present in cells lacking cilia or flagella. This analysis was performed by double-label immunofluorescence microscopy of several cell lines and by immunoblots of protein fractions. Two of the four anti-tektin antibodies, the antibodies 3-7-1 and 3-10-1, which bind different epitopes of the C-tektin, label 3T3, HeLa, PtK2, and BHK-21 cells as well as myotubes. The antibody 3-7-1 stains intermediate filament structures in the cells and binds vimentin or desmin in preparations of cytoskeletal proteins; whereas the antibody 3-10-1 stains nuclear envelopes in the cells and binds lamin A and C in preparations of cytoskeletal proteins or nuclear lamina. Structural similarities between the C-tektin and intermediate filament proteins probably are extended to more than two epitopes because polyclonal antibodies anti-vimentin and anti-desmin bind to C-tektin. These polyclonal antibodies also bind to A-tektin. The cross-reaction of monoclonal and polyclonal antibodies binding to epitopes in tektin and intermediate filament components and the existence of a high content of alpha-helical structure in the tektin subunits (Linck, R. W., and G. L. Langevin, 1982, J. Cell Sci., 58:1-22) indicate that tektin and intermediate filaments are homologous in several parts of their structure.

Trichinella spiralis: antigenic epitopes from the stichocytes detected in the hypertrophic nuclei and cytoplasm of the parasitized muscle fibre (nurse cell) of the host

Parasitology ◽  
1991 ◽  
Vol 102 (1) ◽  
pp. 117-123 ◽  
Author(s):  
D. L. Lee ◽  
R. C. Ko ◽  
X. Y. Yi ◽  
M. H. F. Yeung
Keyword(s):  
Monoclonal Antibodies ◽  
Muscle Fibre ◽  
Polyclonal Antibody ◽  
Nurse Cell ◽  
Trichinella Spiralis ◽  
Polyclonal Antibodies ◽  
Cell Nuclei ◽  
Negative Results ◽  
Immunocytochemical Techniques ◽  
Antigenic Epitopes

SUMMARYMonoclonal antibodies raised against antigens present in the excretions/secretions (E/S) of larval Trichinella spiralis, polyclonal antibodies raised against E/S and antisera from rabbits and pigs infected with T. spiralis were used in conjunction with immunocytochemical techniques to detect antigens in sections of muscle from mice that had been infected with T. spiralis for 15 or 30 days. The antibodies recognized epitopes in the stichocytes, on the surface of the cuticle, in the lumen of the oesophagus and in the lumen of the intestine of encysted larvae. Monoclonal antibodies 7C2C5 and 1H7 and the polyclonal antibodies recognized epitopes in the cavity occupied by the larva, in the cytoplasm of the nurse cell, and in the hypertrophic nuclei of the nurse cell, but did not recognize material in the smaller nuclei of the nurse cell, in the cyst wall or in the surrounding muscle. Monoclonals 3B2E6 and 1D11G8B2, which recognized epitopes in the stichocytes and on the surface of the cuticle of the larvae, gave negative results with the cytoplasm and nuclei of the nurse cell. A polyclonal antibody raised against Trichuris suis recognized epitopes in the muscle and hypodermis of encysted T. spiralis but gave negative results with material in the nurse cell and nurse cell nuclei. The possibility that the antigen detected in the cytoplasm and nuclei of the nurse cell is produced by the stichocytes of the nematode and that it is controlling genes of the altered muscle fibre, either directly or indirectly, is discussed.

Monoclonal and polyclonal antibodies compared for radioimmunoassay of somatomedin-C in patients with acromegaly or hypopituitarism.

1987 ◽  
Vol 33 (9) ◽  
pp. 1593-1596 ◽  
Author(s):  
J M Burrin ◽  
J L Paterson ◽  
P S Sharp ◽  
T H Yeo
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Polyclonal Antibody ◽  
Polyclonal Antibodies ◽  
Detection Limits ◽  
Healthy Adults ◽  
Somatomedin C ◽  
Lower Detection

Abstract We used a synthetic recombinant analog of somatomedin-C (Sm-C) to directly compare the performance of polyclonal and monoclonal antibodies for measuring Sm-C in serum of normal persons and in acromegalic or hypopituitary patients. Mean concentrations of Sm-C in healthy adults were 181 (SD 42) micrograms/L as measured with the monoclonal antibody, 194 (SD 61) micrograms/L with the polyclonal antibody. Both antisera gave excellent discrimination between acromegalics and normals. However, the assay with the polyclonal antibody was more sensitive than that with the monoclonal antibody (lower detection limits: 5 vs 100 micrograms/L) and thus better suited for quantifying Sm-C in samples from hypopituitary patients.

scholarly journals A polyclonal antibody preparation with Michaelian catalytic properties

1991 ◽  
Vol 279 (3) ◽  
pp. 871-881 ◽  
Author(s):  
G Gallacher ◽  
C S Jackson ◽  
M Searcey ◽  
G T Badman ◽  
R Goel ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Polyclonal Antibody ◽  
Polyclonal Antibodies ◽  
Catalytic Antibodies ◽  
Initial Assessment ◽  
Compound I ◽  
Keyhole Limpet Haemocyanin ◽  
Antibody Preparation ◽  
Lower Limits ◽  
Hydrolysis Of

1. 4-Nitrophenyl 4′-(3-aza-2-oxoheptyl)phenyl carbonate (I), an amide conjugate (XI) involving the carboxy group of 4-nitrophenyl 4′-carboxymethylphenyl phosphate and an amino group of keyhole-limpet haemocyanin, and a fluorescein derivative (XVII) were synthesized. 2. The conjugate (XI) was used as an immunogen with which to raise polyclonal antibodies in multigeneration cross-bred sheep; the fluorescent derivative (XVII) was used for the initial assessment of the antisera via binding assays monitored by fluorescence polarization; the carbonate ester (I) was used as a chromogenic substrate for the investigation of catalytic activity. 3. The IgG from the antiserum of sheep no. 270 was isolated by Na2SO4 precipitation and chromatography on Protein G-Sepharose. 4. This preparation of IgG catalysed the hydrolysis of the carbonate ester (I); the catalysis at pH 8.0 and 25 degrees C obeyed Michaelis-Menten kinetics with at least 25 turnovers, Km = 3.34 microM, and lower limits for kcat. of 0.029 s-1 and for kcat./Km of 8.77 x 10(3) M-1.S-1, on the unlikely assumption that the concentration of catalytic antibody is provided by twice the total IgG concentration (two sites per molecule); probable estimates of the fraction of the total IgG that is anti-haptenic IgG and of the fraction of this that is catalytically active suggest that the values of kcat./Km are actually very much larger than these lower limits. 5. The failure of the antibody preparation to catalyse the hydrolysis of the isomeric 2-nitrophenyl carbonate (II), which differs from compound (I) only in the position of the nitro substituent in the leaving group, compels the view that catalytic activity is due to antibody rather than contaminant enzyme; this conclusion is supported by (a) the failure of the following to discriminate effectively between the isomeric substrates (I) and (II): pig liver carboxylesterase, rabbit liver carboxylesterase (collectively EC 3.1.1.1), whole serum from a non-immunized sheep and whole serum from a sheep immunized with a derivative of 3-O-methylnoradrenaline and (b) the lack of catalytic activity in IgG preparations from sheep immunized with sulphoxide or sulphone analogues of immunogen (XI). 6. The various parameters used for the comparison of the kinetic characteristics of hydrolytic catalytic antibodies are discussed. 7. The characteristics of hydrolysis of compound (I) catalysed by the present polyclonal antibody preparation are shown to be substantially better in most respects than those of analogous reactions of two other carbonate esters catalysed by monoclonal antibodies.

An Immunoradiometric Assay for Factor VIII Related Antigen (VIIIRAg) Using Two Monoclonal Antibodies-Comparison with Polyclonal Rabbit Antibodies for Use in von Willebrand’s Disease Diagnosis

1984 ◽  
Vol 52 (03) ◽  
pp. 250-252 ◽  
Author(s):  
Y Sultan ◽  
Ph Avner ◽  
P Maisonneuve ◽  
D Arnaud ◽  
Ch Jeanneau
Keyword(s):  
Monoclonal Antibodies ◽  
Structural Changes ◽  
Polyclonal Antibodies ◽  
Disease Diagnosis ◽  
Immunoradiometric Assay ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Structural Abnormalities ◽  
Antigenic Material ◽  
Von Willebrand

SummaryTwo monoclonal antibodies raised against FVIII/von Willebrand protein were used in an immunoradiometric assay (IRMA) to measure this antigen in normal plasma and plasma of patients with different forms of von Willebrand’s disease. The first antibody, an IgG1 was used to coat polystyrene tubes, the second one, an IgG2a, iodinated and used in the second step. Both antibodies inhibit ristocetin induced platelet agglutination and react strongly with platelets, megacaryocytes and endothelial cells. The IRMA test using these antibodies showed greater sensitivity than that using rabbit polyclonal anti VIIIRAg antibodies. A good correlation between the two tests was nevertheless found when VIIIRAg was measured in the majority of patient’s plasma. However 5 patients from 3 different families showed more antigenic material in the rabbit antibody IRMA than in the monoclonal antibody IRMA. It is suggested therefore that the monoclonal antibodies identify part of the VIIIR:Ag molecule showing structural abnormalities in these vWd patients, these structural changes remaining undetected by the polyclonal antibodies.

Evaluation of germ plasm for resistant to Soybean mosaic virus (SMV)

2020 ◽  
Vol 21 (1) ◽  
pp. 6-9
Author(s):  
Wuye Ria Andayanie
Keyword(s):  
Abiotic Stress ◽  
Environmental Factors ◽  
Mosaic Virus ◽  
Polyclonal Antibody ◽  
Symptom Severity ◽  
Germ Plasm ◽  
Polyclonal Antibodies ◽  
Soybean Mosaic Virus ◽  
High Yield ◽  
High Yields

Soybean superior varieties with high yields and are resistant to abiotic stress have been largely released, although some varieties grown in the field are not resistant to SMV. In addition, the opportunity to obtain lines of hope as prospective varieties with high yield and resistance to SMV is very small. The method for evaluating soybean germplasm is based on serological observations of 98 accessions of leaf samples from SMV inoculation with T isolate. The evaluation results of 98 accessions based on visual observations showed 31 genotypes reacting very resistant or healthy to mild resistant category to SMV T isolate  with a percentage of symptom severity of 0 −30 %. Among 31 genotypes there are 2 genotypes (PI 200485; M8Grb 44; Mlg 3288) with the category of visually very resistant and resistant, respectively and  Mlg 3288  with the category of mild resistant.  They have a good agronomic appearance with a weight of 100 seeds (˃10 g) and react negatively with polyclonal antibodies to SMV, except Mlg 3288 reaction is not consistent, despite the weight of 100 seeds (˃ 10 g). Leaf samples from 98 accessions revealed various symptoms of SMV infection in the field. This diversity of symptoms is caused by susceptibility to accession, when infection occurs, and environmental factors. Keywords—: soybean; genotipe; Soybean mosaic virus (SMV); disease severity; polyclonal  antibody

Immunofluorescence Assay Using Monoclonal and Polyclonal Antibodies for Detection of Staphylococcal Enterotoxins A in Milk

2019 ◽  
Vol 13 (1) ◽  
pp. 137-145 ◽  
Author(s):  
Tzonka Godjevargova ◽  
Zlatina Becheva ◽  
Yavor Ivanov ◽  
Andrey Tchorbanov
Keyword(s):  
Monoclonal Antibody ◽  
Magnetic Nanoparticles ◽  
Polyclonal Antibody ◽  
Polyclonal Antibodies ◽  
Food Poisoning ◽  
Staphylococcal Enterotoxin ◽  
Staphylococcal Enterotoxin A ◽  
Fluorescence Immunoassay ◽  
Magnetic Separator ◽  
Milk Samples

Objectives: Staphylococcus aureus is a Gram-positive microorganism. S. aureus can grow in various foods and cause food poisoning by secreting enterotoxins. The most common enterotoxins involved in food poisoning are staphylococcal enterotoxin A and staphylococcal enterotoxin B, but Staphylococcal Enterotoxin A (SEA) is predominant. The main types of food contaminated with SEs are meat and meat products, poultry and eggs, milk and dairy products. The aim of this study was to develop a rapid and sensitive fluorescence immunoassay for detection of staphylococcal enterotoxin A in milk. Methods: Monoclonal and polyclonal antibodies for SEA were produced and characterized. Competitive fluorescence immunoassay based on Magnetic Nanoparticles (MNPs) was performed and optimized. MNPs were used as a solid carrier of the antibodies. The first step of the assay was immunoreaction between the immobilized antibody onto MNPs and SEA in milk sample. Then the fluorescein-SEA conjugate was added to the sample. Thus, competitive immunoreaction between MNP-mAb/MNP-pAb with SEA and SEA-FITC was performed. These immuno-complexes were separated by a magnetic separator and the obtained supernatants were analyzed. The fluorescent signal from the excess of conjugated SEA was proportional to the SEA contained in the milk. The assay duration was only 30 min. Results: The fluorescence immunoassays performed with polyclonal antibody had linear ranges from 5 pg/mL to 100 ng/mL SEA in a buffer, and from 50 pg/mL to 50 ng/mL SEA in spiked milk samples. While the same assays performed with monoclonal antibody had linear ranges from 1 pg/mL to 20 ng/mL SEA in buffer, and from 10 pg/mL to 10 ng/mL SEA in spiked milk samples. The detection limits of the developed immunoassays performed in milk were: 48 pg/mL with polyclonal antibody and 9 pg/mL with monoclonal antibody. Conclusion: A rapid and sensitive fluorescence immunoassay based on magnetic nanoparticles with a polyclonal and monoclonal antibody for determination of staphylococcal enterotoxin A in milk was developed.

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