scholarly journals Interference of freeze-dried Hepatitis A vaccine (H2 strain) on testing bovine serum albumin content by ELISA

2013 ◽  
Vol 2 (2) ◽  
pp. 21
Author(s):  
Yueqing Chen ◽  
Jun Chen ◽  
Zhuo Chen ◽  
Feng Zhang ◽  
Hualiang Xia ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Glutamic Acid ◽  
Recovery Rate ◽  
Bovine Serum ◽  
Hepatitis A ◽  
Interference Effects ◽  
Elisa Kit ◽  
Freeze Dried ◽  
Albumin Content

<p><strong>Objective</strong> To carry on preliminary research on interference effects of freeze-dried attenuated Hepatitis A vaccine（H2 strain）on testing residual Bovine Serum Albumin content by ELISA kit. <strong>Methods</strong> Interference test was conducted according to Appendix VIII, Chinese Pharmacopoeia (Vol III,2010 edi), and the interference level and its possible resources were explored.<strong> Results</strong> The protective additives of HAV live vaccine do have certain interference on determining residual BSA content by ELISA kit, among which Cysteine and Glutamic acid might play the leading roles. The general BSA recovery rate is 54% to 85%. We assessed the interference degree by using series of different concentration of single amino acid ingredient: cysteine (0 to 0.2%),glutamic acid(0 to 0.8%). We found BSA recovery rate always higher than 70% with 0 to 2mg/ml (0.2%) cysteine, lower with 0.5 to 2mg/ml than with 0 to 0.5mg/ml and did not differ between 0.5 and 2mg/ml cysteine; And the BSA recovery rates were up to 100% if we applied Glutamic acid (concentration not higher than 0.1%) as an interference. It deserves to be mentioned that the interference effects of Glutamic acid become more stronger along with concentration rising from 0.1% to the peak 0.8%(8mg/ml),the test results showed to be not higher than 2.5ng/ml when we set 20ng/ml BSA standards as a target sample, so that the recovery rate is not more than 12.5%. <strong>Conclusion</strong> The real value of residual BSA content of HAV vaccine should be reported based on the extent of interference. Here when the result appeared to be negative by ELISA we would report as &lt;2.5 ng/ml and as &lt; 5ng/ml if the testing value showed between 0 and 3ng/ml. And what we have done might be a reference to the other enterprises on optimizing the protocol for cryopreservation or evaluating the residual BSA content results.</p>

Cytokine mRNA expression in unilateral ischemic-reperfused rat lung with salt solution supplemented with low-endotoxin or standard bovine serum albumin

2004 ◽  
Vol 286 (1) ◽  
pp. L137-L142 ◽  
Author(s):  
Shu Teng ◽  
Shunichi Kurata ◽  
Iyoko Katoh ◽  
Gabriela S. Georgieva ◽  
Toshihisa Nosaka ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Mrna Expression ◽  
Vascular Permeability ◽  
Bovine Serum ◽  
Left Lung ◽  
Rat Lung ◽  
Cytokine Mrna ◽  
Cytokine Mrna Expression ◽  
Albumin Content

Our aim was to determine whether cytokine mRNA expression is induced by experimental manipulation including artificial perfusate or ischemia-reperfusion (I/R) in an isolated, perfused rat lung model. Constant pulmonary flow [Krebs-Henseleit solution supplemented with lowendotoxin (LE) or standard (ST) bovine serum albumin 4%, 0.04 ml/g body wt] and ventilation were maintained throughout. Right and left pulmonary arteries were isolated, and the left pulmonary artery was occluded for 60 min and then reperfused for 30 min. Analysis of tumor necrosis factor-α, IL-1β, IL-6, IL-10, and IFN-γ mRNA expression by RT-PCR and evaluation of vascular permeability by bronchoalveolar lavage (BAL) fluid albumin content were conducted separately in right and left lung. Both LE and ST groups (each 12 rats) showed increases in vascular permeability by I/R (BAL fluid albumin content: 5.53 ± 1.55 vs. 15.63 ± 8.87 and 4.76 ± 2.71 vs. 16.72 ± 4.85 mg·ml BAL fluid-1·g lung dry wt-1, mean ± SD; right vs. left lung in LE and ST groups, P < 0.05 between right and left). Cytokine mRNA expression was significantly higher in the I/R lung than in the control lung in the LE group, whereas it was higher in the control lung in the ST group ( P < 0.05). mRNAs of not only proinflammatory but also anti-inflammatory cytokines were expressed in I/R lung, which are expected to aggravate I/R injury. The reversed pattern of cytokine mRNA expression in the ST group was possibly due to the longer perfusion of control lung with perfusate containing endotoxin, which caused no lung damage without I/R.

Neonatal tolerization with glutamic acid decarboxylase but not with bovine serum albumin delays the onset of diabetes in NOD mice

Diabetes ◽  
1994 ◽  
Vol 43 (12) ◽  
pp. 1478-1484 ◽  
Author(s):  
J. S. Petersen ◽  
A. E. Karlsen ◽  
H. Markholst ◽  
A. Worsaae ◽  
T. Dyrberg ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Glutamic Acid ◽  
Glutamic Acid Decarboxylase ◽  
Bovine Serum ◽  
Nod Mice ◽  
Acid Decarboxylase ◽  
Onset Of Diabetes

Electron spectroscopic imaging of isolated myocardial cells prepared by slam-freeze molecular distillation processing

1990 ◽  
Vol 48 (3) ◽  
pp. 774-775
Author(s):  
Robyn Rufner ◽  
Rebecca C. Stearns ◽  
Cindy L. Hastings ◽  
Steven Borzak ◽  
John J. Godleski
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molecular Distillation ◽  
Spectroscopic Imaging ◽  
Myocardial Cells ◽  
Electron Spectroscopic Imaging ◽  
Sprague Dawley ◽  
Freeze Dried

Isolated adult rat ventricular myocytes serve as a well-defined model to study subcellular events associated with cardiac ischemia. Optimal ultrastructural preservation of in vivo and cultured myocardial cells has been approached by cryo-preservation techniques involving rapid freezing and subsequent freeze substitution or freeze-dried cryosections. Alterations in biochemical structure and composition inherent with chemical fixation procedures can be alleviated by molecular distillation drying of cryo-fixed specimens. In this morphological study, the effects of metal-mirror cryofixation and molecular distillation processing of myocardial cells was evaluated using electron spectroscopic imaging.Myocardial cells were isolated from the ventricles of adult female Sprague-Dawley rats by enzymatic digestion. Briefly, perfused ventricles were minced and incubated with calcium-free Krebs-Henseleit buffer containing 0.05% collagenase and 0.03% hyaluroxidase with 0.002% deoxyribonuclease II and 0.002% trypsin and 1 mM Ca for 10-20 min at 37° with continuous oxygenation and shaking. The tissue was transferred to KH-enzyme buffer plus 2% bovine serum albumin, filtered through Nitex mesh, sedimented by centrifugation (150xg) and then resuspended in 1 mM Ca KH buffer with 2% bovine serum albumin. The yield of viable cells was greater than 70%.

scholarly journals A simple method for non-denaturing purification of biotin-tagged proteins through competitive elution with free biotin

BioTechniques ◽  
2020 ◽  
Vol 68 (1) ◽  
pp. 41-44
Author(s):  
Kui Lin ◽  
Qin Yan ◽  
Audrey Mitchell ◽  
Natasha Funk ◽  
Catherlin Lu ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Purification ◽  
Recovery Rate ◽  
Bovine Serum ◽  
Protein Denaturation ◽  
Simple Method ◽  
Agarose Beads ◽  
Elution Buffer ◽  
Neutral Conditions

The use of avidin or streptavidin in the purification of biotinylated proteins has been highly restricted due to the harsh and denaturing elution conditions. Here, we use biotinylated bovine serum albumin as a working model to demonstrate a simple and rapid method for biotin-tagged protein purification under non-denaturing conditions. The biotinylated bovine serum albumin is specifically bound to the anti-biotin antibody agarose beads and competitively eluted with free biotin under near-neutral conditions. The optimized elution conditions include using 4 mg/ml biotin (pH 8.5) as the elution buffer and allowing the buffer to incubate with agarose beads for 30 min prior to elution. The elution recovery rate is over 85% without apparent protein denaturation. The method is applicable for both immunoprecipitation and column chromatography.

Neonatal Tolerization With Glutamic Acid Decarboxylase But Not With Bovine Serum Albumin Delays the Onset of Diabetes in NOD Mice

Diabetes ◽  
1994 ◽  
Vol 43 (12) ◽  
pp. 1478-1484 ◽  
Author(s):  
J. S. Petersen ◽  
A. E. Karlsen ◽  
H. Markholst ◽  
A. Worsaae ◽  
T. Dyrberg ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Glutamic Acid ◽  
Glutamic Acid Decarboxylase ◽  
Bovine Serum ◽  
Nod Mice ◽  
Acid Decarboxylase ◽  
Onset Of Diabetes

Chrysin-loaded bovine serum albumin particles as bioactive nanosupplements

2020 ◽  
Vol 11 (7) ◽  
pp. 6007-6019 ◽  
Author(s):  
Joana B. Ferrado ◽  
Adrián A. Perez ◽  
Maria C. Ruiz ◽  
Ignacio E. León ◽  
Liliana G. Santiago
Keyword(s):  
Breast Cancer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Cancer Cells ◽  
Bovine Serum ◽  
Breast Cancer Cells ◽  
Freeze Dried ◽  
Induced Apoptosis

Freeze-dried Chrys-loaded BSAnp retained their properties after reconstitution and induced apoptosis on breast cancer cells. BSAnp-70-11 (smallest sized) was the most cytotoxic system with a gastrointestinal release of 14% Chrys.

Lack of a synergistic effect of arginine–glutamic acid on the physical stability of spray-dried bovine serum albumin

2016 ◽  
Vol 22 (6) ◽  
pp. 785-791 ◽  
Author(s):  
Mouhamad Reslan ◽  
Yusuf K. Demir ◽  
Bernhardt L. Trout ◽  
Hak-Kim Chan ◽  
Veysel Kayser
Keyword(s):  
Bovine Serum Albumin ◽  
Synergistic Effect ◽  
Serum Albumin ◽  
Glutamic Acid ◽  
Bovine Serum ◽  
Physical Stability ◽  
Spray Dried

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.

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