Results 291 to 300 of about 1,355,358 (352)

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 ...
S, Carballal, B, Alvarez, L, Turell, H, Botti, B A, Freeman, R, Radi   +5 more
openaire   +2 more sources

Human Serum Albumin−Mercurial Species Interactions

Journal of Proteome Research, 2007
Binding of metal ions to the heteroatomic sites of proteins is undoubtedly fundamental to their observed physiological effects. In this paper, the interactions of inorganic mercury (Hg2+), methylmercury (MeHg+), ethylmercury (EtHg+), and phenylmercury (PhHg+) with human serum albumin (HSA) were studied from the electrophoretic behaviors, stoichiometry,
Yan, Li, Xiu-Ping, Yan, Chen, Chen, Yun-Long, Xia, Yan, Jiang   +4 more
openaire   +2 more sources

Human Serum Albumin on Fluorinated Surfaces

Langmuir, 2003
The aim of this work is to investigate the stabilization of the conformation of adsorbed human serum albumin (HSA) on surfaces containing CF3 and/or OH groups. These groups are structural characteristics (mimics) of trifluoroethanol, which is known to stabilize the secondary structure of several proteins.
Coelho, M., Vieira, E., Motschmann, H., Möhwald, H., Thünemann, A.   +4 more
openaire   +2 more sources

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.
K J, Fehske, E, Jähnchen, W E, Müller, A, Stillbauer   +3 more
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Polymerized soluble venom—Human serum albumin

Journal of Allergy and Clinical Immunology, 1985
Extensive previous studies have demonstrated that attempts to produce polymers of Hymenoptera venoms for human immunotherapy resulted in insoluble precipitates that could be injected with safety but with very limited immunogenicity in allergic patients.
R, Patterson, I M, Suszko, L C, Grammer
openaire   +2 more sources

The characterization of two specific drug binding sites on human serum albumin.

Molecular Pharmacology, 1975
The binding of a number of fluorescent probe molecules to human serum albumin (HSA) has been studied. Small changes in the amino acid moiety of the dansylamino acids resulted in large changes in the binding of these compounds to HSA. It is suggested that
Gillian Sudlow, D. Birkett, D. Wade
semanticscholar   +1 more source

Flavonoid binding to human serum albumin

Biochemical and Biophysical Research Communications, 2010
Dietary 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, M. Marino, G. Rimbach, FANALI, GABRIELLA, FASANO, MAURO, P. Ascenzi   +5 more
openaire   +5 more sources

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, P, Wahl
openaire   +2 more sources

Resveratrol Binding to Human Serum Albumin

Journal of Biomolecular Structure and Dynamics, 2006
Resveratrol (Res), a polyphenolic compound found largely in the skin of red grape and wine, exhibits a wide range of pharmaceutical properties and plays a role in prevention of human cardiovascular diseases [Pendurthi et al., Arterioscler. Thromb. Vasc. Biol. 19, 419-426 (1999)].
C N, N' soukpoe-Kossi, C, St-Louis, M, Beauregard, M, Subirade, R, Carpentier, S, Hotchandani, H A, Tajmir-Riahi   +6 more
openaire   +2 more sources

Temperature Behaviour of Human Serum Albumin

European Journal of Biochemistry, 1980
Structural alterations of albumin, their dependence on concentration and the role of free --SH groups at thermal denaturation, as well as the reversibility of thermally induced structural changes, were studied. Application of various physical methods provides information on a series of structural parameters in a major concentration range.
R, Wetzel, M, Becker, J, Behlke, H, Billwitz, S, Böhm, B, Ebert, H, Hamann, J, Krumbiegel, G, Lassmann   +8 more
openaire   +2 more sources