Protection against Klebsiella pneumoniae induced lobar pneumonia in rats with lipopolysaccharide and related antigens

1990 ◽  
Vol 36 (12) ◽  
pp. 885-890 ◽  
Author(s):  
Mamta Rani ◽  
Rajesh K. Gupta ◽  
S. Chhibber
Keyword(s):  
Bovine Serum Albumin ◽  
Klebsiella Pneumoniae ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Lipid A ◽  
Bacterial Colonization ◽  
Lobar Pneumonia ◽  
Key Words Lipopolysaccharide ◽  
Shwartzman Reaction ◽  
High Concentrations

The immunoprotective role of lipopolysaccharide and related antigens from Klebsiella pneumoniae was studied in a lobar pneumonia model developed in rats. Various antigens were obtained by different chemical treatments of the lipopolysaccharide. All these antigens (purified lipopolysaccharide, reduced lipopolysaccharide, lipopolysaccharide – bovine serum albumin complex, and lipid A – bovine serum albumin complex were tested for pyrogenicity and the Shwartzman reaction. The lipopolysaccharide and the various related antigens were pyrogenic and elicited a positive Shwartzman reaction at high concentrations. However, at low concentrations, the same preparations did not show any side effects. All these antigens, on the other hand, were protective against bacterial challenge in Klebsiella pneumoniae induced lobar pneumonia in rats, as the bacterial colonization of lungs in the immunized animals was significantly lower when compared with the controls. The alveolar macrophages from these animals also showed significantly more uptake of Klebsiella pneumoniae as compared with those obtained from control animals. Key words: lipopolysaccharide, vaccine, pneumonia, protection.

Interaction of Bis-Guanidinium Acetates Surfactants with Bovine Serum Albumin Evaluated by Spectroscopy

2021 ◽  
Vol 58 (3) ◽  
pp. 187-194
Author(s):  
Yongbo Song ◽  
Yulan Niu ◽  
Hongyan Zheng ◽  
Ying Yao
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cd Spectroscopy ◽  
Binding Characteristics ◽  
Low Concentrations ◽  
Quenching Efficiency ◽  
Hydrophobic Chain ◽  
Upward Curvature ◽  
High Concentrations

Abstract The interactions between cocopropane bis-guanidinium acetates, tallowpropane bis-guanidinium acetates with bovine serum albumin (BSA) in an aqueous solution were studied by fluorescence and circular dichroic spectroscopy measurements. The aim of the study was to elucidate the influence of the hydrophilic group and the length of the hydrophobic chain of these surfactants on the mechanism of binding to BSA. The results revealed that for both surfactants, at low concentrations, the Stern–Volmer plots had an upward curvature and at high concentrations, the quenching efficiency was decreased with increase in surfactant concentration. Different thermodynamics parameters demonstrated the existence of hydrogen bond and van der Waals force which acting as binding forces. Static quenching was observed among the protein and surfactant. The conformation of BSA was changed at higher surfactant concentrations as shown by synchronous fluorescence and CD spectroscopy. This work reveals the mechanism and binding characteristics between guanidine surfactants and protein, and provided the basis for further applications of surfactants.

scholarly journals STUDIES ON ANTIBODY PRODUCTION

1963 ◽  
Vol 117 (6) ◽  
pp. 1035-1051 ◽  
Author(s):  
Maria C. Michaelides ◽  
Albert H. Coons
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Antibody Formation ◽  
Culture Fluid ◽  
Antibody Responses ◽  
Plasma Clot ◽  
Anamnestic Response ◽  
Hind Foot ◽  
High Concentrations

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.

scholarly journals Biological Activities of Lipid A Complexed with Bovine-Serum Albumin

1972 ◽  
Vol 31 (2) ◽  
pp. 230-233 ◽  
Author(s):  
Chris Galanos ◽  
Ernst T. Rietschel ◽  
Otto Luderitz ◽  
Otto Westphal ◽  
Yoon B. Kim ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Lipid A ◽  
Biological Activities

scholarly journals Pyrogenicity and Immunogenicity of Lipid A Complexed with Bovine Serum Albumin or Human Serum Albumin

1973 ◽  
Vol 8 (2) ◽  
pp. 173-177 ◽  
Author(s):  
E. T. Rietschel ◽  
Y. B. Kim ◽  
D. W. Watson ◽  
C. Galanos ◽  
O. Lüderitz ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
Lipid A

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.

RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diethyl Ether ◽  
Bovine Serum ◽  
Domestic Fowl ◽  
Laying Hens ◽  
Peripheral Plasma ◽  
The Mean ◽  
Precision And Accuracy ◽  
Chicken Ovary

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.

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