Results 291 to 300 of about 650,535 (339)
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Food anaphylaxis to bovine serum albumin
Journal of Allergy and Clinical Immunology, 1998Although 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 ...
Cécile de Hauteclocque +2 more
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Disulfide-bond scrambling promotes amorphous aggregates in lysozyme and bovine serum albumin.
Journal of Physical Chemistry B, 2015Disulfide bonds are naturally formed in more than 50% of amyloidogenic proteins, but the exact role of disulfide bonds in protein aggregation is still not well-understood.
Mu Yang, Colina Dutta, A. Tiwari
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Immunochemistry of Bovine Serum Albumin
1978Two 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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Interaction of acrylamide with bovine serum albumin
Environmental Research, 1986The binding of acrylamide (ACR) with purified bovine serum albumin (BSA) was studied. Binding of ACR with BSA was characterized by equilibrium dialysis, fluorescence studies, and ultraviolet spectroscopy. ACR was quantitated by high-pressure liquid chromatography.
Prahlad K. Seth +3 more
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The interaction of rivanol with bovine serum albumin
Archives of Biochemistry and Biophysics, 1961Abstract 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.
Abraham Saifer +2 more
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Adsorption of bovine serum albumin on glass
Biochimica et Biophysica Acta, 1956Abstract 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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Interaction of wogonin with bovine serum albumin
Bioorganic & Medicinal Chemistry, 2005The 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
Jiaqin Liu +3 more
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The binding of atropine to bovine serum albumin
Biochemical Pharmacology, 1962Abstract The binding of atropine to bovine serum albumin (BSA) as a model system was studied by ultrafiltration, spectrophotometry, and biological assay. Binding of atropine increased with an increase in pH from 5 to 8; the number of binding sites was approximately 20 at pH 6 and 100 at pH 8. Exhaustively acetylated BSA still bound some atropine when
Stephen I. Oroszlan +1 more
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Binding of noradrenaline to bovine serum albumin
International Journal of Nuclear Medicine and Biology, 1981Abstract 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 ...
Y. Cohen, E. Rodriguez Farre
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Complexes of Dendrimers with Bovine Serum Albumin
Biomacromolecules, 2010We report the complexation of bovine serum albumin (BSA) with several dendrimers of different compositions mPEG-PAMAM (G3), mPEG-PAMAM (G4), and PAMAM (G4) at physiological conditions using constant protein concentration and various dendrimer contents.
J. S. Mandeville +1 more
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