Results 231 to 240 of about 468,755 (304)
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Raman studies of bovine serum albumin

Biopolymers, 1976
AbstractThe Raman Spectra of bovine serum albumin have been obtained in the solute state, in alkaline and acidic solutions, and in the gel. The reversible denaturations of bovine serum albumin solutions by heat, acid's, and alkali were studied and a new mechanism for heat denaturation has been proposed based on a continuous unfolding of the α‐helices.
V J, Lin, J L, Koenig
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THE COMBINATION OF HEPARIN AND BOVINE SERUM ALBUMIN

Canadian Journal of Medical Sciences, 1953
The complexing of heparin and bovine serum albumin in acetate buffer at pH 5.0 was studied by electrophoretic techniques. A stable complex with a heparin : albumin mole ratio of 1 : 2 was found, though there was evidence for the existence of unstable complexes with a higher heparin : albumin ratio.
D W, CLARKE, F C, MONKHOUSE
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Ionization of Bovine Serum Albumin Monolayers

Nature, 1952
IT has long been known that the surface electrical potential of a protein monolayer at the air/water interface is dependent on the pH and the nature of the ions present in the aqueous sub-solution. There is no record, however, of a comprehensive investigation of the variation of protein surface potential with the pH of the sub-solution.
M Z, DOGAN, J, GLAZER
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Food anaphylaxis to bovine serum albumin

Journal of Allergy and Clinical Immunology, 1998
Although rare, anaphylaxis has been reported after topical administration of bacitracin ointment.1-7 All reported patients, including ours, had applied the drug to a compromised skin barrier (i.e., leg ulcers, excoriated dermatitis, or burns). Thus ready access to the systemic circulation seems to be a prerequisite for the development of anaphylaxis ...
G, Kanny   +2 more
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On the aggregation of bovine serum albumin

Journal of Molecular Liquids, 2022
Abstract In an attempt to elucidate the aggregation behaviour of bovine serum albumin and its modulation by salt ions, size-exclusion high-performance liquid chromatography was used and complemented by dynamic light scattering. The influence of the protein concentration, and type and concentration of inorganic salt on the aggregation of albumin in ...
Madeira, Pedro P.   +4 more
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The interaction of rivanol with bovine serum albumin

Archives of Biochemistry and Biophysics, 1961
Abstract Interaction of the cationic form of rivanol (6, 9-diamino-2-ethoxyacridine lactate) with native and modified bovine serum albumins (BSA) was studied by various physicochemical methods. Influence of pH and ionic strength on precipitation of BSA by rivanol was investigated.
G, KALDOR, A, SAIFER, F, VECSLER
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Interaction of wogonin with bovine serum albumin

Bioorganic & Medicinal Chemistry, 2005
The binding of wogonin with bovine serum albumin (BSA) was investigated at different temperatures by fluorescence, circular dichroism (CD) and Fourier transform infrared spectroscopy (FT-IR) at pH7.40. The association constants K were determined by Stern-Volmer equation based on the quenching of the fluorescence of BSA in the presence of wogonin, which
Jianniao, Tian   +3 more
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Immunochemistry of Bovine Serum Albumin

1978
Two fragments were isolated from BSA one was derived from the first terminal third of the molecule and the second from the last third of the molecule. Each fragment inhibited the reaction of BSA-anti BSA by 90% or better. An immunoabsorbent of each bound 90% of anti BSA. Each fragment bound two antibody molecules per mole of fragment. These results are
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Adsorption of bovine serum albumin on glass

Biochimica et Biophysica Acta, 1956
Abstract 1. 1. The adsorption of bovine serum albumin on powdered pyrex glass has been studied as a function of protein concentration and of pH at an ionic strength of 0.05 and at 30°C. 2. 2. The surface area of the pyrex glass powder has been calibrated with the use of microscopic spherical glass particles. 3. 3. The limiting area of the
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Binding of noradrenaline to bovine serum albumin

International Journal of Nuclear Medicine and Biology, 1981
Abstract The binding of noradrenaline to bovine serum albumin (40 mg ml −1 ) has been studied by gel filtration. Over the range of 5 × 10 −9 M to 10 −3 M of noradrenaline, the data obtained fit a model with three classes of noninteracting binding sites: a high affinity-low capacity site with a K A of 1.18 × 10 6 M −1 and a capacity of 11.84 ...
E R, Farre, Y, Cohen
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