Results 281 to 290 of about 737,493 (351)

Effect of heating and ionic strength on the interaction of bovine serum albumin and the antinutrients tannic and phytic acids, and its influence on in vitro protein digestibility.

Food Chemistry, 2018
Bioavailability of food nutrients can be reduced in the presence of antinutrients such as phytates and tannins. This work aimed to study bovine serum albumin binding to phytic acid and tannic acid, and its influence on in vitro protein digestibility. The
Elaine Kaspchak, Luciana Igarashi Mafra, M. R. Mafra   +2 more
semanticscholar   +1 more source

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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Complexes of Dendrimers with Bovine Serum Albumin

Biomacromolecules, 2010
We 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, H A, Tajmir-Riahi
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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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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, C, de Hauteclocque, D A, Moneret-Vautrin   +2 more
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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, Jiaqin, Liu, Zhide, Hu, Xingguo, Chen   +3 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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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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Conjugate of bovine serum albumin with nicotine

Biochemical and Biophysical Research Communications, 1974
Abstract The preparation and characterization of a nicotine-albumin conjugate are reported. The nicotine derivative, 6-(p-aminobenzamido)nicotine, which was coupled to bovine serum albumin(BSA), was synthesized by the following sequence; 1 -nicotine→6-aminonicotine→6-(p-nitrobenzamido)nicotine→6-(p-aminobenzamido)nicotine.
H, Matsushita, M, Noguchi, E, Tamaki
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