Enzyme-Linked Immunosorbent Assay for Streptomycin in Animal Feeds

2013 ◽  
Vol 651 ◽  
pp. 280-283
Author(s):  
Hui Ying Zhang ◽  
Jun Ping Wang
Keyword(s):  
Detection Limit ◽  
Bovine Serum Albumin ◽  
Immunosorbent Assay ◽  
Polyclonal Antibody ◽  
Bovine Serum ◽  
Enzyme Linked Immunosorbent Assay ◽  
Animal Feeds ◽  
Inhibition Concentration ◽  
Coefficients Of Variation ◽  
Bovine Serum Albumin Conjugate

Polyclonal antibody against streptomycin was prepared by using a streptomycin–bovine serum albumin conjugate for the immunization of rabbits. Using this antibody, we developed quantitative assays for streptomycin by means of an indirect competitive enzyme-linked immunosorbent assay (icELISA). Fifty percent inhibition concentration (IC50) for the antibody was 3.6 ng/ml. The detection limit was 0.4 ng/ml. The average of recoveries for all samples was 86.14% and the coefficients of variation of intra- and inter-assays were below 18%. The detection limit using the kit was 15 ng/ml in animal feeds.

scholarly journals Easy Enzyme-Linked Immunosorbent Assay for Spectinomycin in Chicken Plasma

1996 ◽  
Vol 79 (2) ◽  
pp. 426-430 ◽  
Author(s):  
Touichi Tanaka ◽  
Hideharu Ikebuchi ◽  
Jun-Ichi Sawada ◽  
Mariko Okada ◽  
Yasumasa Kido
Keyword(s):  
Detection Limit ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Immunosorbent Assay ◽  
Bovine Serum ◽  
Cross Reactivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Carrier Protein ◽  
Bovine Serum Albumin Conjugate

Abstract An easy, sensitive, competitive indirect enzyme- linked immunosorbent assay (CI-ELISA) for specti nomycin in chicken plasma was developed. Preparation of a spectinomycin-bovine serum albumin conjugate in which the hapten is linked to the carrier protein through the C-4 position is described. Antibodies raised against antigens in rabbits had excellent specificity for spectinomycin, exhibiting a cross-reactivity of 44.0% with dihydrospectinomy-cin and 13.8% with tetrahydrospectinomycin. No cross-reactivity was observed with other antibiotics. The detection limit of the CI-ELISA was 2 ng/mL (equivalent into 40 ng/mL undiluted chicken plasma) spectinomycin. Known amounts (0.1-100 μg/mL) of spectinomycin were added to chicken plasma and then analyzed. Average recoveries were 97-110%. This procedure may be used without prior extraction of samples.

scholarly journals Enzyme-linked immunosorbent assay for the determination of isoflavones in alimentary important plants

2004 ◽  
Vol 22 (SI - Chem. Reactions in Foods V) ◽  
pp. S199-S202 ◽  
Author(s):  
M. Vítková ◽  
Z. Macková ◽  
R. Koblovská ◽  
O. Lapčík
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Medicago Sativa ◽  
Immunosorbent Assay ◽  
Polyclonal Antibody ◽  
Bovine Serum ◽  
Enzyme Linked Immunosorbent Assay ◽  
Acceptable Range ◽  
Carboxy Methyl

The development of polyclonal antibody-based enzyme-linked immunosorbent assays (ELISA) for the determination of individual isoflavones, i.e. daidzein, genistein and biochanin and their homologues, is presented in this work. Isoflavone conjugates with bovine serum albumin were used as immunogens, coupled at the position C 7 and C 4’ via a carboxy methyl spacer. The developed ELISAs are highly specific, I<sub>50</sub> values of the standard curves range between 0.3–1.2 ng/ml. The cross reactivities to other isoflavones are in acceptable range and the interference of non-isoflavonoid molecules is negligible. The immunoassays have been used for monitoring of changes in isoflavone levels in alimentary important plants, such as Medicago sativa, during germination; and during different vegetation stages of the Rutaceae family plants.

scholarly journals KONJUGASI ANHIDRAT KlORAMFENIKOL-PROTEIN (CAP-BSA DAN CAP-KLH) UNTUK PRODUKSI IgG DARI SERUM KELINCI

2011 ◽  
Vol 1 (2) ◽  
pp. 23-31
Author(s):  
Musyirna Rahmah Nst ◽  
Tri Budhi Murdiati
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Immunosorbent Assay ◽  
Bovine Serum ◽  
Keyhole Limpet Hemocyanin ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein Bovine Serum Albumin

 Dalam pengembangan metoda analisis residu antibiotik pada produk pangan hewani secara immunokimia telah dilakukan sintesis imunogen kloramfenikol (CAP) dengan protein Bovine Serum Albumin (BSA) dan Keyhole Limpet Hemocyanin (KLH) dengan metoda konjugasi mixed anhidrad. Hasil sintesis digunakan untuk produksi antibodi.Antigen dan antibodi yang dihasilkan dijadikan prangkat analisis residu antibiotik dengan Competitive Enzyme Linked Immunosorbent Assay (ELISA kompetitif). Hasil penelitian menunjukkan bahwa metoda konjugasi mixed anhidrad pada preparasi imunogen dengan jumlah CAP yang terkonjugasi ke grup amino bebas dari molekul protein BSA (CAP-BSA) adalah 18 unit dan ke protein KLH (CAP-KLH) adalah 782 unit. Antibodi poliklonal CAP-BSA dan CAP-KLH yang diproduksi dengan rata-rata kandungan IgG CAP-BSA 2,07 mg/ml dan IgG CAP-KLH 2,21 mg/ml.

Lack of specificity of current anti-digoxin antibodies, and preparation of a new, specific polyclonal antibody that recognizes the carbohydrate moiety of digoxin.

1985 ◽  
Vol 31 (10) ◽  
pp. 1625-1631 ◽  
Author(s):  
B Thong ◽  
S J Soldin ◽  
C A Lingwood
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Polyclonal Antibody ◽  
Bovine Serum ◽  
Lactone Ring ◽  
Cross Reactivity ◽  
Carbohydrate Moiety ◽  
Reductive Ozonolysis ◽  
Bovine Serum Albumin Conjugate ◽  
Specific Polyclonal Antibody

Abstract Current immunoassays for digoxin do not distinguish digoxin from its glycosidic metabolites. We have synthesized a novel digoxin/bovine serum albumin conjugate via reductive ozonolysis of the lactone ring such that the carbohydrate moiety of digoxin remains intact. Antibodies raised against this conjugate show minimal cross reactivity to digoxigenin, bisdigitoxide, monodigitoxide, digoxigenin, and digitoxin. With this antibody, digoxin can be measured in the presence of these metabolites.

Enzyme-linked immunosorbent assay for 17 alpha-hydroxyprogesterone in dried blood spotted on filter paper.

1987 ◽  
Vol 33 (6) ◽  
pp. 761-764 ◽  
Author(s):  
M Maeda ◽  
H Arakawa ◽  
A Tsuji ◽  
Y Yamagami ◽  
A Isozaki ◽  
...  
Keyword(s):  
Detection Limit ◽  
Immunosorbent Assay ◽  
Filter Paper ◽  
Cost Effective ◽  
Enzyme Linked Immunosorbent Assay ◽  
Adrenal Hyperplasia ◽  
Bovine Serum Albumin Conjugate ◽  
Enzyme Conjugate ◽  
Sensitivity Specificity ◽  
Microwell Plate

Abstract In this rapid, cost-effective, enzyme-linked immunosorbent assay for 17 alpha-hydroxyprogesterone (17-OHP) eluted from dried blood spotted on filter paper, second antibody is coated onto the microwell plate and horseradish peroxidase (EC 1.11.1.7) is the label enzyme. Antiserum to 17-OHP was prepared by using 4-(2-carboxymethylthio)-17-OHP-bovine serum albumin conjugate as immunogen. Enzyme conjugate was prepared from 4-(2-carboxymethylthio)-17-OHP and peroxidase. The blood spots are assayed in the microwells without extraction or centrifugation steps. The detection limit of the assay is 1 microgram/L, equivalent to 3.5 pg (10.6 fmol) per disc. Intra- and interassay CVs at two steroid concentrations (7.38 and 22.79 micrograms/L) ranged from 3.74 to 11.90% (n = 5), and 9.49 and 9.83% (n = 5), respectively. Results correlated well (r = 0.91) with those of a fluorescence enzyme immunoassay. The sensitivity, specificity, and precision of this method make it potentially useful in the mass screening of neonates for congenital adrenal hyperplasia.

Production of Monoclonal Antibodies against Diquat and Its Enzyme-Linked Immunosorbent Assay

1993 ◽  
Vol 33 (2) ◽  
pp. 117-120 ◽  
Author(s):  
B Wu ◽  
M Nagao ◽  
K Terazawa ◽  
T Takatori ◽  
H Akabane
Keyword(s):  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Immunosorbent Assay ◽  
Bovine Serum ◽  
Clinical Sample ◽  
Enzyme Linked Immunosorbent Assay ◽  
Spleen Cells ◽  
Myeloma Cells ◽  
Toxicological Analysis

Monoclonal antibodies(MoAbs) very specific to diquat (DQ) were produced. An immunogen was synthesized by binding DQ to bovine serum albumin via a diazo-coupled derivative. BALB/c mice were immunized i.p. monthly with 0.25mg of the immunogen for five months. Their spleen cells were fused with P3U1 myeloma cells and hybridoma clones secreting MoAbs were obtained. Two MoAbs were selected and subtyped to be IgM and IgG3. The MoAbs recognized DQ but did not bind to paraquat and other analogues at all. A datum obtained from a clinical sample demonstrates that an enzyme-linked immunosorbent assay system using one of the MoAbs is useful in the practice of toxicological analysis.

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