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Flavonoid binding to human serum albumin
Biochemical and Biophysical Research Communications, 2010Dietary flavonoid may have beneficial effects in the prevention of chronic diseases. However, flavonoid bioavailability is often poor probably due to their interaction with plasma proteins. Here, the affinity of daidzein and daidzein metabolites as well as of genistein, naringenin, and quercetin for human serum albumin (HSA) has been assessed in the ...
A. Bolli +5 more
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Biotechnology and Applied Biochemistry, 1996
Recombinant human albumin produced in the yeast Saccharomyces cerevisial and human serum albumin derived from blood fractionation were compared by a series of analytical techniques. These demonstrated that the two proteins were equivalent structurally. However, differences observed in some of the assays indicated that the recombinant product had lower ...
Alan Victor Quirk +5 more
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Recombinant human albumin produced in the yeast Saccharomyces cerevisial and human serum albumin derived from blood fractionation were compared by a series of analytical techniques. These demonstrated that the two proteins were equivalent structurally. However, differences observed in some of the assays indicated that the recombinant product had lower ...
Alan Victor Quirk +5 more
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Stabilization of Human Albumin by Caprylate and Acetyltryptophanate
Vox Sanguinis, 1984Abstract. The thermal stabilization of human albumin by caprylate (CA) and acetyltryptophanate (AT) was studied by monitoring the formation of albumin polymer (defined as species larger than dimer) on the basis of its molecular size as well as its characteristic migration as α‐globulin.
M.W. Yu, J.S. Finlayson
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Stereoselective binding of human serum albumin
Chirality, 2006AbstractStereoselectivity in binding can have a significant effect on the drug disposition such as first‐pass metabolism, metabolic clearance, renal clearance, and protein and tissue binding. Human serum albumin (HSA) is able to stereoselectively bind a great number of various endogenous and exogenous compounds. Various experimental data suggested that
Chuang, Victor, Otagiri, M.
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Dissociation of Human Albumin Dimer by Heating
Vox Sanguinis, 1974Abstract. Exclusion chromatography was used to prepare human albumin dimer from normal serum albumin (human) which had been heated repeatedly at 56 °C and from un‐heated fraction V which had been treated with ethanol and dried at 25 °C. When these purified dimer preparations were heated in solution for 10 h at 60°C in the presence of acetyltryptophan ...
B. L. Reamer +2 more
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Rotational and translational dynamics of human albumin
Physical Review A, 1986Laser-light-scattering and electron-spin-resonance spectroscopies have been used to measure the translational and the rotational diffusion coefficients of human albumin. In the framework of the Debye-Stokes-Einstein theory, the two coefficients yielded two significantly different values for the hydrodynamics radius of the biomolecule.
S. Cannistraro, SACCHETTI, Francesco
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Genetics of Albumin Gainesville, a New Variant of Human Serum Albumin
Nature, 1969A “NEW” slow-moving variant of serum albumin has been found in members of a single family of Irish descent from the vicinity of Gainesville, Florida1. We have demonstrated that the electrophoretic mobility of albumin Gainesville is different from the mobilities of previously reported slow-moving albumins2–5, and have provided evidence to support the ...
Thomas Lau +4 more
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Spectrophotometric Titrations of Human Serum Albumin and Reduced Carboxymethylated Albumin
Science, 1963The tyrosyl groups of reduced and carboxymethylated human serum albumin, in which all disulfide bonds are broken, ionize at lower p H than those of native albumin, in spite of the greater negative charge on the protein produced by the S-carboxymethyl groups.
David Eisenberg, John T. Edsall
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Drug binding sites on chicken albumin: a comparison to human albumin
Journal of Veterinary Pharmacology and Therapeutics, 1997Mammalian albumins have two main structurally selective ligand binding sites. Site I binds drugs such as azapropazone, phenylbutazone and warfarin; whereas benzodiazepines, some dansyl amino acids, such as dansylsarcosine, and short chain fatty acids like octanoic acid interact with site II.
Christopher J. Bowmer +2 more
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