Albumin infusion improves renal function in cirrhosis; however, mechanisms are incompletely understood. In clinical practice, human albumin is used in various intensive care unit indications to deal with a wide range of problems, from volume replacement in hypovolemic shock, or sepsis, to treatment of ascites in patients with liver cirrhosis. Against the background of the results of recent stud...

A comparative study of the ligand-binding properties of human serum albumin was performed by the technique of affinity chromatography with the protein attached to immobilized Cibacron Blue F3GA (Blue Sepharose), or covalently immobilized on Sepharose. The binding strength of octanoate, decanoate and dodecanoate is much weaker when human serum albumin is attached to immobilized Cibacron Blue, in...

Albumin, the most abundant protein in vertebrate serum, is thought to be a nonessential protein because other serum proteins take over albumin’s actions to bind and transport hydrophobic ligands such as fatty acids, bilirubin, and steroids and to maintain osmotic pressure in blood in “analbuminemic” humans (Gitlin and Gitlin 1975; Bowman et al. 1976) and rats (Nagase et al. 1979). Additional su...

Infection and increased systemic inflammation cause organ dysfunction death in patients with decompensated cirrhosis. Preclinical studies provide support for an antiinflammatory role of albumin, but confirmatory large-scale clinical trials are lacking. Whether targeting a serum albumin level 30 g per liter or greater these repeated daily infusions 20% human solution, as compared standard care, ...

Human liver sections were stained with anti-human serum albumin and/or anti-human fibrin monomer fluorescent conjugates. Approximately 10 per cent of the hepatic cells stained specifically for human serum albumin,1 per cent for fibrinogen, and 0.1 per cent for both. Approximately 18 per cent of the Kupffer cells stained specifically for human serum albumin and 33 per cent for fibrinogen. Staini...

Objective: To study the role of peroxynitrite-modified human serum albumin (nitroxidized-albumin) in rheumatoid arthritis. Methods: Human serum albumin was exposed to peroxynitrite and changes in albumin structure were monitored by UV-visible, fluorescence and circular dichroism spectroscopy, thioflavin T, Congo red binding and attenuated total reflection-Fourier transformed infrared spectrosco...

A rapid method for nearly quantitative isolation of human serum albumin is described. The present technic (1) is a modification of the Schwert method (2). In the present method 4 ml. of serum is precipitated with trichloroacetic acid in a final concentration of 5% (w/v). The precipitate is washed with TCA, and after aqueous suspension, ethanol is added to a final concentration of 80%. The undis...

Our goal was to determine whether chlorpyrifos oxon, dichlorvos, diisopropylXuorophosphate (DFP), and sarin covalently bind tohuman albumin. Human albumin or plasma was treated with organophosphorus (OP) agent at alkaline pH, digested with pepsin at pH2.3, and analyzed by matrix-assisted laser desorption/ionization time-of-Xight (MALDI-TOF) mass spectrometry. Two singly chargedpeaks...

The antigenic structure of human albumin was investigated in order to establish whether or not there was any similarity between its antigenic sites. Using immunoadsorbent columns prepared with cyanogen bromide fragments of human serum albumin, antibodies directed against different portions of the albumin molecules were isolated. Measurement of the amount of the antibodies isolated and study of ...