Plasma Cells and their Precursors III. Late Phases of anti-Bovine Serum Albumin IgG Antibody Responses Depend upon Newly Produced IgG B-Memory Cells

Immunobiology ◽  
1983 ◽  
Vol 164 (1) ◽  
pp. 68-77 ◽  
Author(s):  
E. Veenhoff ◽  
A. Zwart ◽  
P.H. Boer ◽  
H.G. Seijen
1963 ◽  
Vol 117 (6) ◽  
pp. 1035-1051 ◽  
Author(s):  
Maria C. Michaelides ◽  
Albert H. Coons

Rabbits were injected into the hind foot with diphtheria toxoid and bovine serum albumin. Fragments of popliteal lymph node taken from them several months later were placed in plasma-clot cultures with Eagle's medium. When antigen was added to the culture fluid, anamnestic antibody responses occurred regularly. When the antigen was diphtheria, responsiveness remained for 4 days after the beginning of the culture. When it was bovine serum albumin, responsiveness lasted for about 8 days. Once an anamnestic response had begun, antibody formation continued for 4 weeks or more. High concentrations of bovine serum albumin (0.5 mg/ml) did not inhibit the response. When both antigens were used to stimulate the same culture, it was found that the two responses were independent.


1967 ◽  
Vol 125 (3) ◽  
pp. 527-536 ◽  
Author(s):  
Ira Green ◽  
Pierre Vassalli ◽  
Baruj Benacerraf

Genetic nonresponder guinea pigs incapable of an immune response to DNP-PLL alone were immunized with DNP-PLL complexed to ovalbumin or bovine serum albumin. Under these circumstances the animals produce both anti-DNP-PLL antibodies and antibodies directed against the conveyor albumin. Thus immune response to DNP-PLL complexed to conveyor albumin molecules can serve as a simple model of hapten-carrier relationships. To explore these relationships the question whether these two types of antibody are synthesized by the same or by different plasma cells was investigated by a combination of a double immunofluorescent technique and radioautographic localization of radioactive antigen. It was shown that the anti-DNP-PLL antibodies and the antibodies against the carrier albumin molecule were produced in separate cells. No cell-producing antibodies with both specificities were detected out of 526 cells studied.


Sensors ◽  
2020 ◽  
Vol 20 (3) ◽  
pp. 771
Author(s):  
Chia-Hung Lin ◽  
Ming-Jie Lin ◽  
Jie-De Huang ◽  
Yu-Sheng Chuang ◽  
Yu-Fen Kuo ◽  
...  

The sensing properties of immunosensors are determined not only by the amount of immobilized antibodies but also by the number of effective antigen-binding sites of the immobilized antibody. Protein A (PA) exhibits a high degree of affinity with the Fc part of IgG antibody to feasibly produce oriented antibody immobilization. This work proposes a simple method to control the PA surface density on gold nanostructure (AuNS)-deposited screen-printed carbon electrodes (SPCEs) by mixing concentration-varied PA and bovine serum albumin (BSA), and to explore the effect of PA density on the affinity attachment of anti-salbutamol (SAL) antibodies by electrochemical impedance spectroscopy. A concentration of 100 μg/mL PA and 100 μg/mL BSA can obtain a saturated coverage on the 3-mercaptoproponic acid (MPA)/AuNS/SPCEs and exhibit a 50% PA density to adsorb the amount of anti-SAL, more than other concentration-varied PA/BSA-modified electrodes. Compared with the randomly immobilized anti-SAL/MPA/AuNS/SPCEs and the anti-SAL/PA(100 μg/mL):BSA(0 μg/mL)/MPA/AuNS/SPCE, the anti-SAL/PA(100 μg/mL): BSA(100 μg/mL)/MPA/AuNS/SPCE-based immunosensors have better sensing properties for SAL detection, with an extremely low detection limit of 0.2 fg/mL and high reproducibility (<2.5% relative standard deviation). The mixture of PA(100 μg/mL):BSA(100 μg/mL) for the modification of AuNS/SPCEs has great promise for forming an optimal protein layer for the oriented adsorption of IgG antibodies to construct ultrasensitive SAL immunosensors.


Vaccines ◽  
2020 ◽  
Vol 8 (2) ◽  
pp. 257
Author(s):  
Cheng Xu ◽  
Jiehao Xu ◽  
Yu Chen ◽  
Øystein Evensen ◽  
Hetron Mweemba Munang’andu ◽  
...  

Immunoassays are among the frontline methods used for disease diagnosis and surveillance. Despite this, there are no immunoassays developed for the Chinese soft-shelled turtle (Pelodiscus sinensis), which has expanded into large scale commercial production in several Asian countries. One of the critical factors delaying the development of immunoassays is the lack of characterized soft-shelled turtle immunoglobulins. Herein, we used mass spectrometry together with the ProtQuest software to identify the soft-shelled turtle IgM heavy chain in serum, which again was used to produce a polyclonal anti-turtle-IgM in rabbits. Thereafter, the polyclonal anti-turtle-IgM was used as a secondary antibody in an indirect ELISA to evaluate antibody responses of soft-shelled turtles injected with the bovine serum albumin (BSA) model antigen. Our findings show that only turtle immunized with a water-in-oil BSA plus ISA 763A VG adjuvant (SEPPIC, France) emulsion had antibodies detected at 42 days post vaccination (dpv) while turtles injected with phosphate buffered saline (PBS) only as well as turtle injected with BSA dissolved in PBS had no significant antibody levels detected in serum throughout the study period. In summary, our findings show that rabbit polyclonal anti-turtle-IgM produced can be used in ELISA to measure serum antibody responses in immunized soft-shelled turtles. Future studies should explore its application in other immunoassays needed for the disease diagnosis and vaccine development for soft-shelled turtles.


Author(s):  
G. D. Gagne ◽  
M. F. Miller

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.


1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson

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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