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This chapter deals with the purification and characterization of human serum albumin (HSA), anew method of albumin purification from human blood was followed. The characterization was carried out through electrophoresis and spectroscope studies. Facters affecting the absorption have been atudied. The effect of solvent perturbation and pH perturbation were also studied, the results indicats that there are different effects of these solvents (such as ethanol, urea, DMSO, ...etc) on the HSA spectrum. The pH titration of albumin show that about 30% of the tyrosyl residues are located on the…mehr

Produktbeschreibung
This chapter deals with the purification and characterization of human serum albumin (HSA), anew method of albumin purification from human blood was followed. The characterization was carried out through electrophoresis and spectroscope studies. Facters affecting the absorption have been atudied. The effect of solvent perturbation and pH perturbation were also studied, the results indicats that there are different effects of these solvents (such as ethanol, urea, DMSO, ...etc) on the HSA spectrum. The pH titration of albumin show that about 30% of the tyrosyl residues are located on the surface of HSA molecules whereas 70% were buried interior the molectules.
Autorenporträt
Prof.Dr. Sami Al-Mudhaffar FIAS,IAS Has obtained a PhD Degree in Biochemistry in 1967.. He was posted in 1967 on teaching and research assignment at the College of science, University of Basrah, then promoted to assistant Professor, and in 1979 to Professor of Biochemistry.