Results 301 to 310 of about 847,836 (355)
Some of the next articles are maybe not open access.
Human serum albumin in neurodegeneration
Reviews in the Neurosciences, 2022Abstract 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
openaire +2 more sources
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.
openaire +3 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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 +1 more source
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 +1 more source
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.
openaire +3 more sources
Sulfenic acid in human serum albumin
Amino Acids, 2006Sulfenic 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 +5 more
openaire +2 more sources
Human Serum Albumin−Mercurial Species Interactions
Journal of Proteome Research, 2007Binding 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 +4 more
openaire +2 more sources