Author/Authors :
Shahani, Minoo Department of Base Science - Science and Research Branch - Islamic Azad University, Tehran , Daneshi-Mehr, Fatemeh Proteomics Research Center - Shahid Beheshti University of Medical Sciences, Tehran , Tadayon, Roya Proteomics Research Center - Shahid Beheshti University of Medical Sciences, Tehran , Hoseinzade Salavati, Behrooz Proteomics Research Center - Shahid Beheshti University of Medical Sciences, Tehran , Akbar Zadeh-Baghban, Ali-Reza Faculty of Paramedical Sciences - Shahid Beheshti University of Medical Sciences, Tehran, , Zamanian, Abbas Department of Surgery - Faculty of Medicines - Shahid Beheshti University of Medical Sciences, Tehran , Rezaei-Tavirani, Mostafa Faculty of Paramedical Sciences - Shahid Beheshti University of Medical Sciences, Tehran,
Abstract :
Human serum albumin has been used as a model protein for protein folding and ligand binding studies over many decades. Due to its long life period and high concentration in plasma, HSA is highly sensitive to glycation. It is reported that 175 mg/dL glucose concentration is a threshold of kidney activity for the beginning of excretion of glucose. pH denaturation of HSA in absence and presence of different concentrations of glucose is studied and based on the Pace two-state model, the findings are analyzed. In addition, florescence emission data of albumin range in the
period of 300-500 nm was depicted. The amounts of free energy change and [D]1/2 parameters of unfolding in correspond to florescence date indicate that glucose induces fine structural change in human serum albumin. Results showed that 175 mg/dL glucose concentration is a critical point for albumin structural and functional alteration.
Keywords :
Human serum albumin , Glucose , Florescence , pH denaturation , Structura , functional alteration
