Topic
Human serum albumin
About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.
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TL;DR: The receptor for polymerized human as well as chimpanzee serum albumins has been identified on the 55-amino acid polypeptide coded by the pre-S region of hepatitis B virus DNA.
Abstract: The receptor for polymerized human as well as chimpanzee serum albumins has been identified on the 55-amino acid polypeptide coded by the pre-S region of hepatitis B virus DNA. Monoclonal antibodies were raised against a synthetic polypeptide of 19 amino acid residues representing a hydrophilic region of the pre-S amino acid sequence deduced from hepatitis B virus DNA. Sheep erythrocytes fixed with glutaraldehyde were coated with monoclonal antibody against the synthetic polypeptide to develop a hemagglutination assay for pre-S polypeptide. The pre-S polypeptide was detected in the serum containing hepatitis B surface antigen particles along with hepatitis B e antigen, with titers in parallel with those of the receptor for polymerized human serum albumin.
75 citations
TL;DR: This is the first report to demonstrate the catalytic allostericity of HSA through a mechanistic approach and shows a correlation with non-microbial drug resistance as HSA is capable of self-hydrolysis of β-lactam drugs, which is further potentiated by pollutants due to conformational changes in HSA.
Abstract: Structural changes in human serum albumin (HSA) induced by the pollutants 1-naphthol, 2-naphthol and 8-quinolinol were analyzed by circular dichroism, fluorescence spectroscopy and dynamic light scattering. The alteration in protein conformational stability was determined by helical content induction (from 55 to 75%) upon protein-pollutant interactions. Domain plasticity is responsible for the temperature-mediated unfolding of HSA. These findings were compared to HSA-hydrolase activity. We found that though HSA is a monomeric protein, it shows heterotropic allostericity for β-lactamase activity in the presence of pollutants, which act as K- and V-type non-essential activators. Pollutants cause conformational changes and catalytic modifications of the protein (increase in β-lactamase activity from 100 to 200%). HSA-pollutant interactions mediate other protein-ligand interactions, such as HSA-nitrocefin. Therefore, this protein can exist in different conformations with different catalytic properties depending on activator binding. This is the first report to demonstrate the catalytic allostericity of HSA through a mechanistic approach. We also show a correlation with non-microbial drug resistance as HSA is capable of self-hydrolysis of β-lactam drugs, which is further potentiated by pollutants due to conformational changes in HSA.
75 citations
TL;DR: The crystal structure of the HSA-PFOS complex is reported and it is shown that PFOS binds to HSA at a molar ratio of 2:1, which provides a structural mechanism to understand the retention of surfactants in human serum.
Abstract: Perfluorooctane sulfonate (PFOS) is a man-made fluorosurfactant and globally persistent organic pollutant. PFOS is mainly distributed in blood with a long half-life for elimination. PFOS was found mainly bound to human serum albumin (HSA) in plasma, the most abundant protein in human blood plasma, which transports a variety of endogenous and exogenous ligands. However, the structural basis of such binding remains unclear. Here, we report the crystal structure of the HSA-PFOS complex and show that PFOS binds to HSA at a molar ratio of 2:1. In addition, PFOS binding renders the HSA structure more compact. Our results provide a structural mechanism to understand the retention of surfactants in human serum.
75 citations
TL;DR: Human serum albumin has been labelled with a terbium complex by means of a reagent prepared from the bis-cyclic anhydride of diethylenetriamine pentaacetic acid and p-aminosalicylic acid, which combines high fluorescent intensity with stability at high dilution.
Abstract: Human serum albumin has been labelled with a terbium complex by means of a reagent prepared from the bis-cyclic anhydride of diethylenetriamine pentaacetic acid and p-aminosalicylic acid. This reagent combines high fluorescent intensity with stability at high dilution (10–9M). The fluorescent conjugate so produced has been used in a simple fluoroimmunoassay, using human serum albumin as a model analyte.
75 citations
TL;DR: Following removal of albumin and IgG from serum, a significant improvement in the resolution of polypeptide spots detected on two‐dimensional gels is found.
Abstract: ProtoClear is a proprietary technique for clearing albumin and immunoglobulin G (IgG) from human serum samples. Albumin constitutes 57-71% of total serum protein and IgG ranges from 8-26%. Removal of these two proteins alone clears approximately 75% of the total protein present in serum and allows the detection of the remaining proteins that are present in far lower concentrations. ProtoClear effectively removed >95% of human serum albumin (HSA) and >97% of human IgG as measured by an anti-HSA competitive immunoassay and a radial immunodiffusion assay, respectively. ProtoClear was far more specific at removing albumin and IgG than Cibracon Blue Dye chromatography (Cibracon Blue), the typically utilized alternative. Comparing two-dimensional (2-D) gels of serum cleared by either Cibracon Blue or by ProtoClear, it was apparent that Cibracon Blue removed a number of proteins in addition to albumin. Following removal of albumin and IgG from serum, we found a significant improvement in the resolution of polypeptide spots detected on two-dimensional gels.
75 citations