Radioimmunoassay of class-specific antibodies (RIACA): Chicken antibodies to bovine serum albumin

1975 ◽  
Vol 12 (8) ◽  
pp. 699-705
Author(s):  
M Viljanen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Antibodies

Rhamnose modified bovine serum albumin as a carrier protein promotes the immune response against sTn antigen

2020 ◽  
Vol 56 (90) ◽  
pp. 13959-13962
Author(s):  
Han Lin ◽  
Haofei Hong ◽  
Jinfeng Wang ◽  
Chen Li ◽  
Zhifang Zhou ◽  
...  
Keyword(s):  
Immune Response ◽  
Bovine Serum Albumin ◽  
Immune Responses ◽  
Serum Albumin ◽  
Cancer Vaccine ◽  
Bovine Serum ◽  
Vaccine Development ◽  
Carrier Protein ◽  
Antigen Uptake ◽  
Specific Antibodies

Rhamnose and sTn antigen were co-conjugated to bovine serum albumin (BSA) for cancer vaccine development. The immune responses against sTn have been significantly augmented with the involvement of Rha-specific antibodies to enhance antigen uptake.

Radioimmunoassay for 13, 14-dihydro-15-ketoprostaglandin F2α and its application in normo- and anovulatory women

1982 ◽  
Vol 100 (1) ◽  
pp. 98-104 ◽  
Author(s):  
Werner Schlegel ◽  
Jaime Urdinola ◽  
Hermann P. G. Schneider
Keyword(s):  
Menstrual Cycle ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Rapid Method ◽  
Plasma Levels ◽  
Bovine Serum ◽  
Limit Of Detection ◽  
Cross Reactivity ◽  
Specific Antibodies ◽  
Standard Range

Abstract. Highly specific antibodies to 13, 14-dihydro-15-ketoprostaglandin F2α (PGFM) were raised in rabbits. The animals were immunized with PGFM-bovine serum albumin (BSA)-conjugates. Prior to the incubation procedure PGFM was extracted by a rapid method with dichloromethane followed by column chromatography. The antisera dilution was 1:10000 and the cross-reactivity towards prostaglandin A2, E2, F2α, 13, 14-dihydro-15-ketoprostaglandin E2 and the 15-ketoprostaglandin E2 and F2α was < 1%. The limit of detection was 1.9 ± 0.6 pg/ml plasma over the standard range 1.9–250 pg. The intra- and inter-assay variations were 3.9 and 15%, respectively. PGFM was measured throughout the menstrual cycle in female volunteers. In normal ovulatory women (n = 3) plasma levels of PGFM varied between 65.6 to 107.1 pg/ml. No significant variations of plasma PGFM were seen during the cycle. In anovulatory women (n = 4) no difference of PGFM was found during the cycle. PGFM levels in hyperprolactinaemic but ovulating women tend to be higher than in anovulatory, and normoprolactinaemic subjects. These data strongly indicate that PGFM is not correlated with other hormonal parameters tested here in the normal and anovulatory cycles.

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.

Radioimmunoassay of class-specific antibodies (RIACA): Chicken antibodies to bovine serum albumin

1975 ◽  
Vol 12 (8) ◽  
pp. 699-705 ◽  
Author(s):  
Matti K. Viljanen ◽  
Kaisa Granfors ◽  
Paavo Toivanen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Antibodies

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

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