Results 311 to 320 of about 847,836 (355)
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Human Serum Albumin on Fluorinated Surfaces
Langmuir, 2003The 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. +4 more
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Azapropazone binding to human serum albumin
Naunyn-Schmiedeberg's Archives of Pharmacology, 1980Azapropazone, 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 +3 more
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Polymerized soluble venom—Human serum albumin
Journal of Allergy and Clinical Immunology, 1985Extensive 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
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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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Fluorescence studies on human serum albumin
Biochemical and Biophysical Research Communications, 1971Abstract 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
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Resveratrol Binding to Human Serum Albumin
Journal of Biomolecular Structure and Dynamics, 2006Resveratrol (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 +6 more
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Temperature Behaviour of Human Serum Albumin
European Journal of Biochemistry, 1980Structural 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 +8 more
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Adverse Reactions to Human Serum Albumin
Annals of Pharmacotherapy, 1993OBJECTIVE: To describe the adverse effects associated with human serum albumin (HSA) administration. DATA SOURCES: A MEDLINE search and bibliography scanning were used to identify pertinent review articles, clinical studies, and case reports. STUDY SELECTION: Emphasis was placed on reporting the results of human studies with the primary objective of ...
B J, Gales, B L, Erstad
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Albumin Máku: a New Variant of Human Serum Albumin
Nature, 1968AT least six different electrophoretic variants of human serum albumin have been found in man; three migrate more rapidly than normal and three less rapidly1,2. One of these, a rapidly migrating variant, occurs at a frequency of 5–30 per cent in several tribes of North American Indians3.
L R, Weitkamp, N A, Chagnon
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Phase I Comparability of Recombinant Human Albumin and Human Serum Albumin
The Journal of Clinical Pharmacology, 2005Recombinant human albumin (rHA) is a highly purified animal‐, virus‐, and prion‐free product developed as an alternative to human serum albumin (HSA), to which it is structurally equivalent. The present investigation compared the safety, tolerability, and pharmacokinetics/pharmacodynamics of rHA with HSA.
Dietrich, Bosse +6 more
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