Results 271 to 280 of about 492,888 (308)
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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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THE ACYLATION OF BOVINE SERUM ALBUMIN WITH DIACETYLCYCLOSERINE
International Journal of Peptide and Protein Research, 1977The reaction of the amino groups of bovine serum albumin (BSA) with diacetyl‐cycloserine (I) at pH 7.2–9.0 proceeded with both acylation by the diacetyl‐β‐aminooxy‐D‐alanyl (DAA) group and acetylation. The number of DAA groups was determined by their conversion to cycloserine (III) which can be accurately measured in micromolar amounts.
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The binding of ascorbate to bovine serum albumin.
International journal for vitamin and nutrition research. Internationale Zeitschrift fur Vitamin- und Ernahrungsforschung. Journal international de vitaminologie et de nutrition, 1984Ultrafiltration has been used to investigate the interaction of ascorbate with bovine serum albumin in 0.1 M sodium phosphate buffer, pH 6.5. The results are interpreted in terms of the binding of ascorbate to four equivalent and independent protein sites, governed by an intrinsic association constant of 2 600 +/- 700 M-1 at 20 degrees C, thereby ...
Oelrichs B.A. +3 more
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