Using chemical chaperones to increase recombinant human erythropoietin secretion in CHO cell line.

In recombinant protein production, over-expressed genes induce unfolded protein response (UPR), overloaded protein aggregation in endoplasmic reticulum and its expansion. In this study, we have used 16 chemicals to improve erythropoietin production in engineered CHO cells and tried to study the mechanism of reducing protein aggregation in each treatment. Endoplasmic reticulum expansion was studied through endoplasmic reticulum specific labeling with utilizing fluorescent glibenclamide and its molecular chaperones expression were studied by real-time polymerase chain reaction.

Physicochemical screening for chemical stabilizer of erythropoietin to prevent its aggregation.

Recombinant protein aggregation is a problematic issue and can provoke immunological response. The aim of this study was to analyze the stability of erythropoietin (EPO), as a therapeutic protein expressed in mammalian cells, in the presence of different chemicals and find a specific stabilizer for EPO. The effects of several chemicals, including mannitol, betaine, trehalose, taurine, linoleic acid, beta-cyclodextrin, copper sulfate, spermidine, maltose, maltodextrin, sucrose, dextran, beta-alanine, myo-inositol, and cysteine, on protein stabilization through the thermally induced aggregation of EPO were monitored.

An investigation into the parameters affecting preparation of polybutyl cyanoacrylate nanoparticles by emulsion polymerization.

Emulsion polymerization was used to synthesize poly butyl cyanoacrylate nanoparticles in presence of steric stabilizer dextran 70. Nanoparticles were characterized by particle size analysis, scanning electron microscopy and light microscopy. Polymerization factors affecting particle size and distribution such as dextran 70, polysorbate 80 (PS 80) and H(+) concentration, polymerization time and temperature, and sonication were studied.

Production and Purification of Rabbit's Polyclonal Antibody Against Factor VIII.

The attempt is made to produce recombinant factor VIII but the first step in producing such product is production and purification of rabbit's polyclonal antibody against factor VIII. The second and third steps involve monoclonal antibody and recombinant factor VIII production. Factor VIII is one of the most important coagulating factor where its deficiency leads to diseases like hemophilia type A or classic.

Improvement of Desferrioxamine B Production of Streptomyces pilosus ATCC 19797 With Use of Protease Inhibitor and Minerals Related to Its Activity.

The relationship between protease and Desferal production was assayed. Experiments were performed using a cultivation of Streptomyces pilosus ATCC 19797 in soybean broth medium containing 2% soybean flour and 2% mannitol. The metabolism of the trihydroxamic acid sidrophore desferrioxamine B and protease production by a S.