Egg white is one of the important nutrients that frequently induces allergic reactions, particulary in atopic children .The proteins of egg white are common causes of hyper - sensitivity symptoms among atopic individuals so in the way of studying the allergy to egg , it is essential to purify egg white proteins . In the present study, ion exchange chromatography, immune electrophoresis (IE) and polyacrylamid gel electrophoresis (SDS-PAGE) were used for separation and PURIFICATION of egg white proteins. Following ion exchange chromatography, three fractions including: F1, F2, F3 were distinguished and isolated in concrete pHs. The isolated fractions were analysed by SDS - PAGE and IE. The results indicated several protein bands in F1, a single protein band in F2 and a major protein band with minor impurity in F3. Also molecular weight of the isolated fractions was determined by SDS-PAGE, so F2 and F3 identified as ovotransferrin (conalbumin) and ovalbumin respectively. The study indicated that ovotransferrin was highly pure, whereas ovalbumin included a little impurity.

Dendritic cells (DC) are the principal antigen-presenting cells (APC) responsible for induction of primary immune responses by T lymphocytes. Although DCs are present in most lymphoid tissues, they occur in very low frequency accounting for 0.5% or less of nucleated cells in peripheral lymphoid organs. In the present study, we report the PURIFICATION of DCs from mouse spleen with high yield and purity using a three-step PURIFICATION technique including: collagenase digestion of tissue, selection of low-density cells using Optiprep density gradient medium and plastic adherence. By using techniques outlined above, we obtained 5-7×107 DC/spleen with purity of 97%. Such large numbers of purified DCs enables us to further document their different characteristics including morphology, immunophenotype and to evaluation of their role in immune system. Finally, since DCs have been reported to be present in all reproductive organs, we suggest that this protocol be used for isolation and PURIFICATION of DCs from those organs for further in vitro studies.

Lipopolysaccharide (LPS) is one of the most important components of Gram negative bacteria cell walls which form a hydrophobic unit (Lipid A) and a hydrophilic unit (polyssaccharide ). Extraction and PURIFICATION of LPS is an essential step in determination of biochemical, pathophysiological and immunological properties. In the present report the LPS of Salmonella typhimurium PTCC 1735 was extracted and purified. The phenol-water solution method was used to extract the bacterial LPS. Proteins and nucleic acids were removed by means of pronase and nucleases and gel filteration. Crude LPS yield was about 1.8% of initial bacterial dry weight. after gel filteration the content of protein and nucleic acids in LPS preparations were calculated to be 0.2% and 0.5% respectively. Profiles of pure LPS by SDS-PAGE were demonstrated.

Background: Zoonotic cutaneous leishmaniasis (ZCL) is an increasing public health problem in some endemic regions. Horseradish peroxidase (HRP) conjugated rabbit anti-Rhombomys opimus (R. opimus) Ig is needed for immunoblotting and ELISA tests used to explore the immune response of the rodents against the sand fly saliva. In this study, the production of HRP conjugated rabbit anti-R. opimus Ig was conducted for the first time.Methods: Rhombomys opimus Ig was purified from serum by protein G affinity chromatography column and injected into rabbit to produce anti-R. opimus Ig antibody. The titration of antibody against R. opimus Ig in rabbit serum was checked using indirect ELISA. Rabbit anti-R. opimus Ig was purified by Sepharose-4B- R. opimus Ig column. Reactivity of this antibody was assessed by indirect ELISA and was conjugated to HRP by periodate method.Results: Approximately 3.5 mg Ig was purified from 1 ml R. opimus serum using protein G affinity chromatography column. The molecular weight of purified R. opimus Ig was estimated about 150 kDa by SDS-PAGE. Nearly 2.3 mg rabbit anti-R. opimus Ig was purified from 1 ml immunized rabbit serum. The purified antibody was conjugated to HRP and the optimum titer of HRP conjugated rabbit anti-R. opimus Ig was determined as 1: 8000 using direct ELISA.Conclusion: HRP conjugated rabbit anti-Gerbil IgG has been produced by a few companies, but to our knowledge HRP conjugated rabbit anti-R. opimus Ig is not commercially available. Production of HRP conjugated rabbit anti- R. opimusIg is considerably helpful for immunological studies of R. opimus, the main reservoir host of ZCL in Iran as well as some other countries.

An efficient method for PURIFICATION of Yard-Glass Shaped Boron Nitride NanoTubes (YG-BNNTs) fabricated via a Chemical Vapour Reaction (CVR) route has been developed. Impurities including carbon, Boron Nitride (BN), and Fe species in the pristine YG-BNNT sample are removed by a combined physical and chemical procedure which involves ultrasonication, high temperature oxidation, hot-water washing and acid washing. The samples at different stages of the PURIFICATION process are monitored using X-Ray powder Diffraction (XRD), X-ray Photoelectron Spectroscopy (XPS) and Transmission Electron Microscopy (TEM). The results reveal that the carbon and BN impurities could be easily eliminated. However, the catalyst nanoparticles (Fe3C) encaged in the tubes prove to be effectively shielded from oxidation and acid corrosion. Although the content of catalyst nanoparticles could be satisfactorily reduced to about 1.0 wt% by prolonged ultrasonication and acid washing, a small number of such magnetic nanoparticles are still left in the final purified YG-BNNTs. The YG-BNNTs exhibit a typical ferromagnetic behaviour even after a longtime oxidizing and acid washing treatment, indicating that they could be potentially used for harsh-environment magnetic devices.