scholarly journals Surface-bound bovine serum albumin carrier protein as present in recombinant cytokine preparations amplifies T helper 17 cell polarization

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Lei Dong ◽  
Alexandra Helmke ◽  
Ari Waisman ◽  
Hermann Haller ◽  
Andreas Pich ◽  
...  
2020 ◽  
Vol 56 (90) ◽  
pp. 13959-13962
Author(s):  
Han Lin ◽  
Haofei Hong ◽  
Jinfeng Wang ◽  
Chen Li ◽  
Zhifang Zhou ◽  
...  

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.


1996 ◽  
Vol 79 (2) ◽  
pp. 426-430 ◽  
Author(s):  
Touichi Tanaka ◽  
Hideharu Ikebuchi ◽  
Jun-Ichi Sawada ◽  
Mariko Okada ◽  
Yasumasa Kido

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.


1982 ◽  
Vol 35 (3) ◽  
pp. 353-360 ◽  
Author(s):  
E. Diane Williamson ◽  
R. L. S. Patterson

ABSTRACTAn auto-immunization procedure selective for boar 5α-androstenone is described. Immunization of boars with a conjugate of androstenone and bovine serum albumin as a carrier protein significantly reduced the accumulation of androstenone in adipose tissue from a mean value of 0·77 (s.e. 0·19)mg/kg fat for untreated boars to 0·24 (s.e. 0·06) mg/kg fat for treated animals. No detrimental side-effects were observed in the immunized animals, and the advantages of male-type growth and carcass characteristics were preserved.


Immunity ◽  
2021 ◽  
Author(s):  
Yifan Wu ◽  
Zhimin Zeng ◽  
Yubiao Guo ◽  
Lizhen Song ◽  
Jill E. Weatherhead ◽  
...  

CHEST Journal ◽  
2015 ◽  
Vol 147 (6) ◽  
pp. 1610-1620 ◽  
Author(s):  
Aurélie Hautefort ◽  
Barbara Girerd ◽  
David Montani ◽  
Sylvia Cohen-Kaminsky ◽  
Laura Price ◽  
...  

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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