Results 281 to 290 of about 1,355,358 (352)
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Detection Methods and Research Progress of Human Serum Albumin
Critical reviews in analytical chemistry, 2020Human serum albumin (HSA) is a biological macromolecule with important physiological functions; abnormal HSA levels are associated with coronary heart disease, multiple myeloma, diabetes, nephropathy, neurometabolic disorders, liver cirrhosis and other ...
Jian-Fei Xu +3 more
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Recombinant human serum albumin
Drugs of Today, 2007Human serum albumin (HSA) is responsible for 80% of the colloid osmotic pressure of plasma (25-33 mmHg). Its main clinical use is in maintaining colloid oncotic pressure and increasing circulating plasma volume with the typical dosage in excess of 10 g per dose.
Chuang, Victor, Otagiri, M.
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Journal of Molecular Graphics and Modelling, 2020
Serum albumin (SA) is the most abundant protein in blood. SA carries a diverse range of nutrients and drugs. It has wide clinical and biochemical applications.
Sombat Ketrat +2 more
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Serum albumin (SA) is the most abundant protein in blood. SA carries a diverse range of nutrients and drugs. It has wide clinical and biochemical applications.
Sombat Ketrat +2 more
semanticscholar +1 more source
International Journal of Biological Macromolecules, 2019
Human serum albumin (HSA) is an opulent, non-glycosylated, most versatile carrier protein in plasma possessing multiple functions. HSA has the ability to interact with a variety of ligands, including exogenous pharmacological drugs.
G. Rabbani, Saeyoung Ahn
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Human serum albumin (HSA) is an opulent, non-glycosylated, most versatile carrier protein in plasma possessing multiple functions. HSA has the ability to interact with a variety of ligands, including exogenous pharmacological drugs.
G. Rabbani, Saeyoung Ahn
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Dendrimers Bind Human Serum Albumin
The Journal of Physical Chemistry B, 2009Dendrimers 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.
E, Froehlich +4 more
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Structural basis of drug recognition by human serum albumin.
Current Medicinal Chemistry, 2020BACKGROUND Human serum albumin (HSA), the most abundant protein in plasma, is a monomeric multi-domain macromolecule with nine observed binding sites for endogenous and exogenous ligands.
Loris Leboffe +4 more
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Separation of Human Serum Albumins
Nature, 1960THE 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, 1972Abstract 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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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 +4 more
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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 +4 more
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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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