Drug-Protein Conjugates: Preparation of Triamcinolone-Acetonide Containing Bovine Serum Albumin/Keyhole Limpet Hemocyanin-Conjugates and Polyclonal Antibodies

1995 ◽  
Vol 328 (11-12) ◽  
pp. 775-780 ◽  
Author(s):  
Franz Gabor ◽  
Fritz Pittner ◽  
Paul Spiegl
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Triamcinolone Acetonide ◽  
Bovine Serum ◽  
Polyclonal Antibodies ◽  
Keyhole Limpet Hemocyanin ◽  
Protein Conjugates

Synthesis and Characterization of Hapten-Protein Conjugates for Antibody Production against Cyanogenic Glycosides

2015 ◽  
Vol 78 (7) ◽  
pp. 1408-1413 ◽  
Author(s):  
ISLAMIYAT FOLASHADE BOLARINWA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Antibody Titer ◽  
Bovine Serum ◽  
Polyclonal Antibodies ◽  
Enzyme Linked Immunosorbent Assay ◽  
Cyanogenic Glycosides ◽  
Protein Conjugates ◽  
Novel Approach ◽  
Cyanogenic Plants

Consumption of cyanogenic plants can cause serious health problems for humans. The ability to detect and quantify cyanogenic glycosides, capable of generating cyanide, could contribute to prevention of cyanide poisoning from the consumption of improperly processed cyanogenic plants. Hapten-protein conjugates were synthesized with amygdalin and linamarin by using a novel approach. Polyclonal antibodies were generated by immunizing four New Zealand White rabbits with synthesized amygdalin-bovine serum albumin and linamarin-bovine serum albumin immunogen. This is the first time an antibody was produced against linamarin. Antibody titer curves were obtained from all the four rabbits by using a noncompetitive enzyme-linked immunosorbent assay. High antibody titer was obtained at dilutions greater than 1:50,000 from both immunogens. This new method is an important step forward in preventing ingestion of toxic cyanogenic glycosides.

Antibodies to Indolealkylamines; Serotonin and Melatonin

1974 ◽  
Vol 52 (3) ◽  
pp. 196-202 ◽  
Author(s):  
Lee J. Grota ◽  
Gregory M. Brown
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molar Ratio ◽  
Double Immunodiffusion ◽  
Protein Conjugates ◽  
Spectrophotometric Data ◽  
Freund’S Adjuvant ◽  
Freund's Adjuvant

Serotonin, N-acetyl serotonin, and 5-methoxy-N-acetyl serotonin (melatonin) were conjugated to bovine serum albumin (BSA) using formaldehyde. The molar ratio of hapten to protein was determined spectrophotometrically. Spectrophotometric data indicated that serotonin and N-acetyl serotonin but not melatonin were conjugated to bovine serum albumin. Selected hapten–protein conjugates were suspended in Freund's adjuvant and injected into rabbits. Antisera were harvested monthly and screened by double immunodiffusion. Immunodiffusion and inhibition tests indicated that antibodies raised to serotonin–BSA reacted with serotonin and 5-methoxytryptamine but failed to cross react with N-acetyl serotonin or melatonin. Inhibition tests indicated that antibodies to N-acetyl serotonin – BSA reacted with N-acetyl serotonin and cross reacted with melatonin but not with serotonin or 5-methoxytryptamine.

The production of polyclonal antibodies against the mycotoxin derivative patulin hemiglutarate

1993 ◽  
Vol 39 (9) ◽  
pp. 861-863 ◽  
Author(s):  
L. J. McElroy ◽  
C. M. Weiss
Keyword(s):  
Molecular Weight ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Antibody Titer ◽  
Bovine Serum ◽  
Polyclonal Antibodies ◽  
Competitive Elisa ◽  
Low Molecular Weight ◽  
Specific Antibodies ◽  
Indirect Competitive Elisa

The mycotoxin patulin is a toxic, carcinogenic, unsaturated lactone produced by a number of molds. Polyclonal antibodies against patulin hemiglutarate were produced. Specific antibodies against patulin alone, however, were not clearly demonstrated. Because of its low molecular weight, patulin required conjugation to bovine serum albumin (BSA) to increase its immunogenicity. Anti-patulin-hemiglutarate-BSA antibody titer and specificity were determined using indirect and indirect competitive ELISA, respectively. Immunoassays would facilitate detection and quantitation of patulin.Key words: patulin, mycotoxin, antibodies.

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.

scholarly journals COMPETITION OF HASTENS

1966 ◽  
Vol 124 (3) ◽  
pp. 293-306 ◽  
Author(s):  
Alfred A. Amkraut ◽  
Justine S. Garvey ◽  
Dan H. Campbell
Keyword(s):  
Bovine Serum Albumin ◽  
Antibody Response ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Clonal Selection ◽  
Keyhole Limpet Hemocyanin ◽  
Red Cell ◽  
Antibody Titers ◽  
Partial Suppression ◽  
Selection Of

Groups of rabbits were injected with either bovine serum albumin, sheep red cell stroma, or keyhole limpet hemocyanin to which 2,4-dinitrophenyl and/or p-azophenyl arsonate groups had been coupled. Groups of animals received either doubly coupled antigen or an equivalent mixture of singly coupled antigens. Materials were injected intravenously as a solution or subcutaneously and intramuscularly in complete Freund's adjuvant. The presence of dinitrophenyl groups on the immunizing antigen could suppress, partially or completely, the antibody response to p-azophenyl arsonate when this hapten was located on the same molecule. Suppression was dependent on the ratio of haptenic groups on the molecule, appeared to be greatly affected by the method of immunization, and could be demonstrated in all three antigen systems. Partial suppression was manifested in decreased frequency and delayed appearance of the response as well as decreased maximal antibody titers. These findings appear irreconcilable with the possibility of direct clonal selection of antibody-producing cells by unprocessed antigen.

Synthesis and Identification of the Ciprofloxacin Hapten-Protein Conjugates

2013 ◽  
Vol 781-784 ◽  
pp. 1244-1247
Author(s):  
Xuan Yun Huang ◽  
Dong Mei Huang ◽  
Yong Fu Shi ◽  
Bing Feng ◽  
Hui Juan Yu ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sulfonic Acid ◽  
High Sensitivity ◽  
Animal Tissues ◽  
Benzene Sulfonic Acid ◽  
Protein Conjugates ◽  
Optimized Conditions ◽  
Carbodiimide Coupling

In order to generate the specific antibody of small molecular hapten-ciprofloxacin for detecting the Ciprofloxacin residues in edible animal tissues. A modified Carbodiimide coupling method was developed to obtain the immunogenic conjugates through coupling ciprofloxacin with bovine serum albumin in five different proportions. The conjugates were characterized and verified by electrophoresis,the trinitro-benzene-sulfonic acid (TNBS) method and ultraviolet spectra scanning. A quantitative analysis of the density of ciprofloxacin-bovine serum albumin conjugates suggested that a high conjugate density 30:1 could be obtained in the optimized conditions. By immunizing the mice, the antibody showed high sensitivity toward ciprofloxacin with an IC50of 4.69 ng/ml. This study confirmed a practical approach for the ciprofloxacin-bovine serum albumin conjugates, through which the high potent antisera specific for ciprofloxacin hapten can be produced for immunoassay.

scholarly journals Production and Purification of IgY antibodies from egg yolk

2020 ◽  
Vol 3 (3) ◽  
pp. 192-195
Author(s):  
Sao Mai Tran Thi ◽  
Oanh Dang Thi ◽  
Huong Dang Thi ◽  
Long Le Thanh ◽  
Lan Huong Nguyen Thi ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Antibody Production ◽  
High Purity ◽  
Bovine Serum ◽  
Significant Contribution ◽  
Polyclonal Antibodies ◽  
Scientific Research ◽  
Egg Yolk ◽  
Egg Yolks

Polyclonal antibodies from vaccinated mammalian have made a significant contribution to scientific research and diagnosis. The fact that recent technologies allow the production of antibodies in egg yolks laid by hens has led to the development of an alternative to antibody production that is less dangerous to animals. The results of this study showed that it is possible to produce a large amount of IgY antibody to bovine serum albumin (BSA), content of about 8 mg/mL of egg yolk emulsion. The anti-BSA IgY antibodies with high purity and anti-BSA activity.

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