Studies on the biological activity of an insulin-stimulating peptide from a tryptic digest of bovine serum albumin

1986 ◽  
Vol 70 (2) ◽  
Author(s):  
Akemichi Ueno ◽  
Naokatu Arakaki ◽  
Toshiya Oribe ◽  
Yoshiro Takeda
Keyword(s):  
Biological Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Tryptic Digest

Insulin-Stimulating Peptide from a Tryptic Digest of Bovine Serum Albumin: Purification and Characterization1

1985 ◽  
Vol 98 (2) ◽  
pp. 269-278 ◽  
Author(s):  
Akemichi UENO ◽  
Yeong-Man HONG ◽  
Naokatu ARAKAKI ◽  
Yoshiro TAKEDA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Tryptic Digest

scholarly journals Adsorption of bovine serum albumin (BSA) by bare magnetite nanoparticles with surface oxidative impurities that prevent aggregation

2019 ◽  
Vol 97 (8) ◽  
pp. 577-583 ◽  
Author(s):  
Somayeh Rahdar ◽  
Abbas Rahdar ◽  
Shahin Ahmadi ◽  
John F. Trant
Keyword(s):  
Biological Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Magnetite Nanoparticles ◽  
Bovine Serum ◽  
Mammalian Cells ◽  
Particle Diameter ◽  
Resistant Bacteria ◽  
Maximum Adsorption Capacity ◽  
Corona Formation

Bare, uncoated magnetite nanoparticles, synthesized using an electrochemical surfactant-free synthesis, have highly oxidized surfaces that prevent aggregation. These particles have demonstrated highly intriguing biological activity showing extremely potent antibiotic activity against both gram-positive and gram-negative bacteria with little toxicity to rats. This difference in activity could be ascribed to the nature of the protein corona. The kinetics and thermodynamics of the binding of bovine serum albumin (BSA), used as a model serum protein, to these magnetite nanoparticles were analyzed. There is no significant change in particle diameter by dynamic light scattering following adsorption, indicating corona formation does not induce aggregation. The maximum adsorption capacity of the particles was determined to be 300 mg of BSA per gram of magnetite. The particles are able to adsorb 90% of the BSA at protein concentrations as high as 500 mg/L. The adsorption is best described using a pseudo second order model and a Langmuir Type III isotherm model. Thermodynamic analysis showed that the process is entropically driven and is spontaneous at all tested temperatures and conditions. However, it appears to be a weak to moderate physical adsorption. This moderate binding affinity could indicate the differential biological activity of these particles towards bacteria and mammalian cells and further support the contention that these are potentially useful new tools for targeting antibiotic-resistant bacteria.

Insulin-stimulating peptide from tryptic digest of bovine serum albumin

1984 ◽  
Vol 122 (3) ◽  
pp. 1179-1185 ◽  
Author(s):  
Akemichi Ueno ◽  
Naokatu Arakaki ◽  
Hideo Inoue ◽  
Toshiya Oribe ◽  
Yoshiro Takeda
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Tryptic Digest

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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