Results 291 to 300 of about 737,493 (351)
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Binding of naproxen to bovine serum albumin and tryptophan-modified bovine serum albumin
Proceedings / Indian Academy of Sciences, 1987Two 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, 1973Abstract 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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Interaction of ochratoxin A with bovine serum albumin
Archives of Biochemistry and Biophysics, 1971Abstract The interaction of ochratoxin A (OA) with bovine serum albumin (BSA) has been demonstrated by spectrophotometric, spectrophotofluorometric, equilibrium dialysis, and Sephadex gel filtration analyses. Spectrophotometric analysis revealed that the absorption maximum of OA shifts to a longer wavelength (near 395–400 nm) as a result of ...
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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.
R, Dixit, M, Das, P K, Seth, H, Mukhtar
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Immunogenicity of Insolubilized Bovine Serum Albumin
The Journal of Immunology, 1966Summary As compared with soluble bovine serum albumin, the use of the heat-denatured protein as an immunizing antigen in rabbits resulted both in a larger number of responding animals and in markedly higher serum antibody titers. In measuring these titers, it was found that the lower the serum titer, the higher was the ...
A A, Hirata, D H, Sussdorf
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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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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
S I, OROSZLAN, G D, MAENGWYN-DAVIES
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International Archives of Allergy and Applied Immunology, 2009
Delayed type hypersensitivity (DTH) to bovine serum albumin (BSA) and to lipid-conjugated BSA were studied comparatively. Unlike the case of BSA with which no DTH can be detected with native antigen, injection of butyric-conjugated BSA (Bu-BSA) in sensitized mice provokes a typical DTH for an early and limited period.
G, Drach, J, Chen-Marotel
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Delayed type hypersensitivity (DTH) to bovine serum albumin (BSA) and to lipid-conjugated BSA were studied comparatively. Unlike the case of BSA with which no DTH can be detected with native antigen, injection of butyric-conjugated BSA (Bu-BSA) in sensitized mice provokes a typical DTH for an early and limited period.
G, Drach, J, Chen-Marotel
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Thermal aggregation of glycated bovine serum albumin
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2010Aggregation and glycation processes in proteins have a particular interest in medicine fields and in food technology. Serum albumins are model proteins which are able to self-assembly in aggregates and also sensitive to a non-enzymatic glycation in cases of diabetes.
Rondeau, P +5 more
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The binding of penicillins to bovine serum albumin
Biochemical Pharmacology, 1966Abstract The binding of phenoxymethylpenicillin and benzylpenicillin to bovine serum albumin has been studied over the pH range 1·5–10·0 in a variety of buffers. There was a marked reduction in binding above pH 9. The buffers used interfered with binding in the order trismaleate > veronal = chloride > phosphate.
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