Results 281 to 290 of about 650,535 (339)
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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).
S Kishore, Meenakshi Maruthamuthu
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Reproduction, Fertility and Development, 2016
Proper oocyte maturation is crucial for subsequent embryo development; however, oocyte mitochondrial and lipid-droplet behaviour are still poorly understood.
Maite del Collado+8 more
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Proper oocyte maturation is crucial for subsequent embryo development; however, oocyte mitochondrial and lipid-droplet behaviour are still poorly understood.
Maite del Collado+8 more
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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.
M.H. Samitz, Sidney A. Katz
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The heterogeneity of bovine serum albumin
Biochimica et Biophysica Acta (BBA) - General Subjects, 1966Abstract 1. 1. The different components of native and modified bovine serum albumin have been investigated with respect to differences in composition and structure. It was found that native bovine serum albumin is composed of at least 3 components, and that most bovine serum albumin samples contain 4.
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Conjugate of bovine serum albumin with nicotine
Biochemical and Biophysical Research Communications, 1974Abstract 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.
Masao Noguchi+2 more
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Elucidating the interaction of limonene with bovine serum albumin: a multi-technique approach.
Molecular Biosystems, 2015The interaction of Bovine Serum Albumin (BSA) with limonene has been studied by UV-visible spectroscopy, fluorescence spectroscopy and molecular docking, and its effects on protein conformation, topology and stability were determined by Circular ...
S. Chaturvedi+5 more
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Binding of isofraxidin to bovine serum albumin
Biopolymers, 2004AbstractThe binding of isofraxidin to bovine serum albumin (BSA) was studied under physiological conditions with BSA concentration of 1.5×10−6 mol · L−1 and drug concentration in the range of 1.67×10−6 mol · L−1 to 2.0×10−5 mol · L−1. Fluorescence quenching spectra in combination with uv absorption spectroscopy, Fourier transform infrared (FTIR ...
Jiaqin Liu+3 more
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Raman studies of bovine serum albumin
Biopolymers, 1976AbstractThe 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.
Jack L. Koenig, V. J. C. Lin
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THE COMBINATION OF HEPARIN AND BOVINE SERUM ALBUMIN
Canadian Journal of Medical Sciences, 1953The complexing of heparin and bovine serum albumin in acetate buffer at pH 5.0 was studied by electrophoretic techniques. A stable complex with a heparin : albumin mole ratio of 1 : 2 was found, though there was evidence for the existence of unstable complexes with a higher heparin : albumin ratio.
D W Clarke, F C Monkhouse
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Ionization of Bovine Serum Albumin Monolayers
Nature, 1952IT 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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