Results 261 to 270 of about 835,253 (311)

Separation of Human Serum Albumins

Nature, 1960
THE presence of several protein components in human serum albumin was recently demonstrated1–3by two-dimensional zone electrophoresis (filter paper followed by starch gel)4. Their identity with albumin was determined by two-dimensional zone electrophoresis3. The proteins are not related to those described by Knedel4 or by Gitlin et al. 5.
M D, POULIK, W W, ZUELZER, R, MEYER
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Plurality of human serum albumin

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972
Abstract Human serum albumin was subjected to ion-exchange chromatography on DEAE Sephadex A-50 and the eluate was subfractionated by gel filtration. Three major and two minor fractions were recognized. The major fractions were: sulfhydryl-rich monomer, sulfhydryl-poor monomer, and the dimer. Of the minor fractions, one was electrophoretically faster
P K, Shrivastava, H, Goch, K, Zakrzewski
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Imaging Human Serum Albumin

AIP Conference Proceedings, 2011
The human serum albumin is a protein and the size of the object is less than the visible light wavelength, therefore it can not be imaged using optical microscopy. The Atomic Force Microscopy (AFM) is a technique that is currently used to reveal details on surfaces by means of different scanning techniques.
Dan Chicea, Liana Maria Chicea, Radu Chicea, Madalin Bunoiu, Iosif Malaescu   +4 more
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Stereoselective binding of human serum albumin

Chirality, 2006
AbstractStereoselectivity 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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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
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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
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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
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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.
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
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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
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