Urea denaturation of bovine serum albumin at pH 9

The conformational stability of bovine serum albumin (BSA) against urea denaturation was investigated in aqueous solutions both in the absence and presence of buffers. Various buffers differing in polar and nonpolar characters such as sodium phosphate, Tris-HCl, (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid) HEPES and [3-(N-morpholino)propanesulfonic acid] MOPS buffers were used in this study. Urea-induced structural changes were analyzed using different probes, i.e., intrinsic fluorescence, ANS fluorescence and UV-difference spectral signal. Presence of different buffers in the incubation medium offered different degrees of resistance to the protein against urea-induced structural changes compared to those obtained in water (in the absence of buffers). A similar trend of buffer-induced structural resistance was noticed with three different probes. The stabilizing effect of these buffers followed the order: MOPS > HEPES > sodium phosphate > Tris-HCl > water. As found in MOPS and HEPES buffers, the highest stability of BSA can be attributed to the presence of morpholine and piperazine rings, respectively, in their structures. These groups might have produced a hydrophobic environment around the protein surface, thus stabilizing protein conformation against urea denaturation.

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Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100128122 ◽

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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The adsorption of bovine serum albumin at the stainless-steel/aqueous solution interface

Journal of Colloid and Interface Science ◽

10.1016/s0021-9797(84)80018-1 ◽

1984 ◽

Vol 98 (1) ◽

pp. 138-143 ◽

Cited By ~ 4

Author(s):

H VANENCKEVORT ◽

D DASS ◽

A LANGDON

Keyword(s):

Aqueous Solution ◽

Stainless Steel ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Solution Interface

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Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653438 ◽

1981 ◽

Vol 46 (03) ◽

pp. 645-647 ◽

Cited By ~ 28

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.

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

Acta Endocrinologica ◽

10.1530/acta.0.0750133 ◽

1974 ◽

Vol 75 (1) ◽

pp. 133-140 ◽

Cited By ~ 9

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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