By Masaki Otagiri, Victor Tuan Giam Chuang
This e-book provides a complete evaluation of scientific and pharmaceutical functions of human serum albumin (HSA), with updates on structural facets of albumin from the views of X-ray crystallography and NMR, endogenous and exogenous ligand binding of albumin in a number of pathological stipulations, and genetic versions and their phenotypes. fast development and improvement of its functions have ended in impressive effects for which albumin has in actual fact been confirmed to be a strong biomaterial. Contributions from prime overseas specialists during this box exhibit how HSA is utilized to analysis, remedy, medicines, and therapy, with a complete advent of HSA. This quantity will entice scientists in pharmaceutical and clinical study together with pharmaceutical chemists, pharmacokineticists, toxicologists, and biochemists not just in academia but in addition in undefined. Readers can successfully collect the newest wisdom of functions of HSA and its impression on human overall healthiness in one volume.
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Additional resources for Albumin in Medicine: Pathological and Clinical Applications
08 mmol/g HSA) are used to maintain the stability of HSA (Bertolini et al. 2012). To avoid the potential spread of blood pathogens, an alternative to blood-derived HSA, recombinant HSA (rHSA), has been successfully produced using Pichia pastoris, Saccharomyces cerevisiae, or Oryza sativa. Solution of rHSA produced by Pichia pastoris is licensed as Medway® in Japan for the treatment of hypoalbuminemia and hemorrhagic shock. This solution also includes Oct and N-AcTrp as stabilizers. Highly pure commercial HSA solutions (almost 100 %) can be achieved with the current production system.
2005). González-Jiménez and Cortijo, using fluorescence and CD measurements, concluded that HSA is denatured using urea in a single two-state transition with a midpoint at about 6 M urea due to the unfolding of domain II (Gonzalez-Jimenez and Cortijo 2002). Even at a urea concentration of 8 M, some residual structure remains in domain I, where denaturation only takes place when a stronger denaturant, GdnHCl, is added. Different conclusions for the urea-induced denaturation were obtained by Muzammil et al.
Expert Opin Drug Deliv 7:915–925 Oganesyan V, Damschroder MM, Cook KE, Li Q, Gao C, Wu H, Dall’Acqua WF (2014) Structural insights into neonatal Fc receptor-based recycling mechanisms. J Biol Chem 289:7812–7824 Olivieri JR, Craievich AF (1995) The subdomain structure of human serum albumin in solution under different pH conditions studied by small angle X-ray scattering. Eur Biophys J 24:77–84 Peters T Jr (1996) All about albumin: biochemistry, genetics and medical applications. Academic, San Diego Quinlan GJ, Martin GS, Evans TW (2005) Albumin: biochemical properties and therapeutic potential.
Albumin in Medicine: Pathological and Clinical Applications by Masaki Otagiri, Victor Tuan Giam Chuang