Drug comparison and categorizing regarded with human serum albumin from years 2006 to 2012

Human serum albumin [HSA] is the most abundant protein constituent of blood plasma. This protein consists of a single polypeptide chain of 585 amino acid residues, which has many important physiological functions. HSA can bind and carry many drugs, including anticoagulants, tranquilizers, and general Anesthetics. Some technique such as: fluorescence spectroscopy, three-dimensional fluorescence, UV-visible, FT-IR, circular dichroism [CD], X-ray scattering [SAXS] technique and molecular modeling was utilized to investigate the effects of acceptor on conformation of the donor [HSA]. The binding site number n and apparent binding constant K[A] drugs corresponding thermodynamic parameters, the free energy change [DELTA G], enthalpy change [DELTA H], and entropy change [DELTA S] were calculated. The hydrophobic effect, van der Waals forces, hydrogen bond and electrostatic interactions play a major role in stabilizing the complex. More investigation also revealed that these drugs bind to the amino acids on the hydrophobic pocket of HSA and induce changes to the secondary structure of the HSA. In this study for better understanding of HSA-drug interactions, we categorized drugs into ten groups from years 2006 to 2012 and are suggested that two important parameters such as Delta G[0][H20] and [D] [½] can be calculated for each groups and refer to ten categories to finally indicate that fine structural change in human serum albumin

Production of monoclonal antibody against alkylhydroperoxide reductase

Development of a stool antigen immunoassay to detect Helicobacter pylori infection requires monoclonal antibody against the specific antigen. Alkylhydroperoxide reductase [AhpC] of Helicobacter pylori has been described as a specific and unique enzyme for H. pylori and therefore, both H. pylori AhpC and Anti-AhpC could be useful in the development of serologic and stool antigen tests, for detecting and monitoring H. pylori infection. The aims of this study were to prepare a monoclonal antibody against AhpC. Accordingly, The isolation and purification of AhpC from H. pylori were attempted by various techniques including ammonium sulfate precipitation, dialysis, preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution. Furthermore mice were immunized intraperitoneally with homogenized gel containing the AhpC band of protein extract of H. pylori in sodium dodecyl sulfate- polyacrylamide gel electrophoresis. The monoclonal antibody was produced using the hybridoma technique.One-dimensional preparative gel electrophoresis allows a single and short purification step, the high-resolution capacity of this technique leads to a high level of purity of the enzyme and consequently to a very high specificity of the antibody. The high specificity of antibody was identified by immune blotting in which the antibody reacted with the purified AhpC and whole cell protein extract from H. pylori in addition to the intact cells of H. pylori. This approach is simple, time and cost-saving for preparation of monoclonal antibody against AhpC of H. pylori