Results 261 to 270 of about 492,888 (308)

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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Heat treatment modifies the allergenicity of beef and bovine serum albumin

Allergy: European Journal of Allergy and Clinical Immunology, 1998
The effect of heat on the allergenicity of beef and bovine serum albumin was investigated among 10 toddlers skin prick test (SPT)-positive to raw and cooked beef.
Alessandro Fiocchi, P Restani, L Bernardo   +2 more
exaly   +1 more source

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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Binding of naproxen to bovine serum albumin and tryptophan-modified bovine serum albumin

Proceedings / Indian Academy of Sciences, 1987
Two classes of binding sites, a single high-affinity site with an association constant of 4·8×106 M−1 and two low-affinity sites with association constant of about 0·05×106 M−1 have been observed in the interaction of Naproxen with bovine serum albumin (BSA).
Meenakshi Maruthamuthu, S Kishore
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The binding of mercury to bovine serum albumin

Environmental Research, 1973
Abstract Additional studies on the binding of mercury by serum albumin is presented. Data were obtained by radiotracer methods and the technique of equilibrium dialysis. The results showed that mercury is bound at other sites in addition to the carboxyl and sulfydryl groups reported previously.
S A, Katz, M H, Samitz
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