Volume 31 (2020)
Volume 30 (2019)
Volume 29 (2018)
Volume 28 (2017)
Volume 27 (2016)
Volume 26 (2015)
Volume 25 (2014)
Volume 24 (2013)
Volume 23 (2012)
Volume 22 (2011)
Volume 21 (2010)
Volume 20 (2009)
Volume 19 (2008)
Volume 18 (2007)
Volume 17 (2006)
Volume 16 (2005)
Volume 15 (2004)
Volume 14 (2003)
Volume 13 (2002)
Volume 12 (2001)
Volume 11 (2000)
Volume 10 (1999)
Volume 9 (1998)
Volume 8 (1997)
Volume 7 (1996)
Volume 6 (1995)
Volume 5 (1994)
Volume 4 (1993)
Volume 3 (1992)
Volume 2 (1991)
Volume 1 (1990)
Volume 1 (1989)
1. Biophysical Studies on the Interaction of Insulin with a Cationic Gemini Surfactant

P.S. Pourhosseini; M. Pirhaghghi; A.A. Saboury; F. Najafi; H. Ghourchian

Volume 26, Issue 2 , Spring 2015, , Pages 105-115

Abstract
  A novel quaternary ammonium-based cationic gemini surfactant (S6) having 1,6 di-bromo hexane as a spacer, have been used and its interaction with insulin in aqueous solution (pH, 7.40) was investigated by several methods including fluorescence spectroscopy, UV-Vis spectroscopy, circular dichroism, dynamic ...  Read More

2. Probing of the Interaction Between Human Serum Albumin and A New Synthesized Pd(II) Complex Using Spectroscopic Methods

A. Divsalar; S. Khodabakhshian; A.A. Saboury; H. Mansuri-Torshizi; M. Evini

Volume 24, Issue 2 , Spring 2013, , Pages 105-111

Abstract
  Human serum albumin (HSA) is an abundant, multifunctional and nonglycosylated negatively charged plasma protein. HSA ascribed ligand-binding and transport properties, antioxidant functions and enzymatic activities. In the present study, the interaction and side effects of a new designed anti-cancer compound ...  Read More

3. A Thermodynamic Study of the Interaction between Urease and Copper Ions

A.A. Saboury; Elaheh Poorakbar-Esfahani; G. Rezaei-Behbahani

Volume 21, Issue 1 , Winter 2010

Abstract
  A thermodynamic study of copper ions by jack bean urease (JBU) was carried out at two temperatures of 27 and 37?C in Tris buffer (30 mM; pH=7.0) using an isothermal titration calorimetry. There is a set of twelve identical and non-interacting binding sites for copper ions. The intrinsic dissociation ...  Read More