Results 271 to 280 of about 493,813 (294)

Sulfenic acid in human serum albumin

Amino Acids, 2006
Sulfenic acid (RSOH) is a central intermediate in both the reversible and irreversible redox modulation by reactive species of an increasing number of proteins involved in signal transduction and enzymatic pathways. In this paper we focus on human serum albumin (HSA), the most abundant plasma protein, proposed to serve antioxidant functions in the ...
Bruce A. Freeman, Beatriz Alvarez, Rafael Radi, Sebastián Carballal, Lucía Turell, Horacio Botti   +5 more
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Heterogeneity of Human Serum Albumin

Nature, 1945
THE existence of more than one serum albumin in the horse has been demonstrated by chemical fractionation by several workers. We have now examined human serum in the Tiselius electrophoresis apparatus under conditions designed to detect heterogeneity of the albumin fraction, and find that it consists of at least two components.
H. Hoch, C. J. O. R. Morris
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Interaction of isofraxidin with human serum albumin

Bioorganic & Medicinal Chemistry, 2004
This study was designed to examine the interaction of isofraxidin with human serum albumin (HSA) under physiological conditions with drug concentrations in the range of 3.3 x 10(-6) mol L(-1)-3.0x10(-5) mol L(-1) and HSA concentration at 1.5 x 10(-6) mol L(-1).
Zhide Hu, Xuan Tian, Jiaqin Liu, Jianniao Tian, Xingguo Chen   +4 more
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Azapropazone binding to human serum albumin

Naunyn-Schmiedeberg's Archives of Pharmacology, 1980
Azapropazone, a new non-steroidal antiinflammatory drug, is strongly bound to human serum albumin. As revealed by Scatchard analysis, one high-affinity binding site with an association constant of about 1.2 x 10(6)M-1 and two low-affinity binding sites with association constants of about 0.05 x 10(6)M-1 were found.
Eberhard Jähnchen, Klaus J. Fehske, Walter E. Müller, Angelika E. Stillbauer   +3 more
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Dendrimers Bind Human Serum Albumin

The Journal of Physical Chemistry B, 2009
Dendrimers are synthetic, highly branched, spherical macromolecules with nanometer dimensions and potential applications in DNA and drug delivery systems. Human serum albumin (HSA) is a major transporter for delivering several endogenous compounds and drugs in vivo.
Emilie Froehlich, J. S. Mandeville, Heidar-Ali Tajmir-Riahi, R Sedaghat-Herati, C J Jennings   +4 more
openaire   +2 more sources

Interaction of taxol with human serum albumin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Taxol (paclitaxel) is an anticancer drug, which interacts with microtuble proteins, in a manner that catalyzes their formation from tubulin and stabilizes the resulting structures (Nogales et al., Nature 375 (1995) 424-427). This study was designed to examine the interaction of taxol with human serum albumin (HSA) in aqueous solution at physiological ...
H.A. Tajmir-Riahi, J.F. Neault, M. Purcell   +2 more
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Reaction of human serum albumin with aldoses

Carbohydrate Research, 1985
The reaction of human serum albumin (HSA) with aldoses (C3-C6) and acetaldehyde has been studied. U.v. and fluorescent spectra of the HSA-glyceraldehyde and HSA-GlcN adducts reveal yellow chromophores absorbing at 300-350 nm and emitting at 435 nm. However, even limited reaction of HSA with acetaldehyde induced perturbation in the Trp microenvironment.
Gerolamo Delfino, Carlo Queirolo, Giovanni Candiano, Elisabetta Gianazza, Pier Giorgio Righetti, Giuseppe Vecchio, Gian Marco Ghiggeri   +6 more
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Hydrolysis of carbaryl by human serum albumin

Archives of Toxicology, 2004
Human serum (HS) and human serum albumin (HSA) were able to hydrolyse the carbamate carbaryl. Carbarylase activity found in HSA was slightly activated by 1 mM Zn2+, Mn2+, Cd2+, Ni2+ and Na+ and by 0.01 mM Pb2+. The organophosphorus compounds paraoxon and O-hexyl O-2,5-dichlorophenyl phosphoramidate, caprylic acid, palmitic acid and the carboxyl ester p-
Eugenio Vilanova, Victoria Carrera, Miguel A. Sogorb   +2 more
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Binding of cefalotin to human serum albumin

European Journal of Drug Metabolism and Pharmacokinetics, 1984
Binding of cefalotin to human serum albumin was studied in vitro by equilibrium dialysis and the quantitative measurement of cefalotin was made by fluorimetric assay. The binding rate of cefalotin to human serum albumin found to be 61,1%. The determination of drug binding parameters showed a large number of binding sites (n = 9.36) and a moderate ...
J. C. Chaumeil, M. O. Decroix, B. Flouvat   +2 more
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Fluorescence studies on human serum albumin

Biochemical and Biophysical Research Communications, 1971
Abstract The fluorescence decay of the tryptophan emission of human serum albumin has been measured in various conditions. In all the cases studied a complex decay is observed, which can be described by a sum of two exponentials. At pH 5.5, the decay times are 3.3 ns and 7.8 ns; the relative contributions of the exponentials being 0.66 and 0.33. This
W.B. de Lauder, Ph. Wahl
openaire   +3 more sources