Results 261 to 270 of about 493,813 (294)
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Human serum albumin in neurodegeneration

Reviews in the Neurosciences, 2022
Abstract Serum albumin (SA) exists in relatively high concentrations, in close contact with most cells. However, in the adult brain, except for cerebrospinal fluid (CSF), SA concentration is relatively low. It is mainly produced in the liver to serve as the main protein of the blood plasma.
Sajjad Shojai   +3 more
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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   +2 more
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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.
R. Meyer, W. W. Zuelzer, M. D. Poulik
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Recombinant human serum albumin

Drugs of Today, 2007
Human 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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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   +5 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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Interaction of Bishydroxycoumarin with Human Serum Albumin

Journal of Pharmaceutical Sciences, 1971
Abstract The binding of bishydroxycoumarin to human serum albumin was studied by means of spectrophotometry, solubility analysis, and equilibrium dialysis. The data were interpreted on the basis of the theory of multiple equilibria. The human serum albumin-bishydroxycoumarin association is exothermic and occurs spontaneously under the experimental ...
A.G. Mitchell, M. Pernarowski, M.J. Cho
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Binding of teicoplanin to human serum albumin

European Journal of Clinical Pharmacology, 1987
The interaction between the main components of the new glycopeptide antibiotic teicoplanin, A2-2, A2-3, A2-4, A2-5 and A3-1, and human serum albumin has been studied in vitro by equilibrium dialysis (pH 7.4, 37 degrees C). From Scatchard analysis of the data, the calculated association constants (Ka) were: A2-2, 2.47 X 10(4), A2-3, 2.86 X 10(4), A2-4 ...
A. Bernareggi, A. Assandri
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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   +4 more
openaire   +2 more sources

Interaction of cimetidine with human serum albumin

Biochemical Pharmacology, 1990
Ultrafiltration studies have detected the existence of a weak interaction between cimetidine and human serum albumin, a finding supported by corresponding studies with this xenobiotic and bovine serum albumin. Furthermore, the binding characteristics of the interaction with human serum albumin (4 sites, K = 630 M-1) more than suffice to account for the
Wilson, Craig J.   +2 more
openaire   +4 more sources

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