In this study, multi wall carbon nanotubes (MWCNTs) were synthesized by Chemical vapor deposition (CVD) method using two different catalysts (Fe nanoparticles) and (Ni nanoparticles) with two different substrates: Quartz and Alumina. Acetylene gas was used as a carbon source and Argon as a carrier gas at different temperatures and different times to study the effects of these parameters on CNTs yield. The produced MWCNTs were then purified by oxidation followed by chemical method involving treatment of MWCNTs with concentrated acids (H2SO4 and HNO3) to remove impurities. The MWCNTs were then functionalized by acidic treatment. The functionalized MWCNTs were then coated with Nickel using electroless plating method. Metal matrix composites (MMCs) were prepared by powder metallurgy method using Al/uncoated MWCNTs and Al/coated MWCNTs. The results show that the diameter range of prepared MWCNTs was (30-50) nm. The yield of CNTs using Ni nanoparticles as catalyst is higher than that of using Fe nanoparticles as catalyst. The coated CNTs have diameters ranging from 65-85 nm. The hardness of Al/coated CNTs composites is higher than that of Al/uncoated MWCNTs composites.

Background and purpose: Lactoferrin is a multifunctional protein, which is useful for clinical and commercial applications. Recently it has been shown that ingestion of Lactoferrin has advantages including: immune system modulation, anti-microbial activity and antioxidant in neonates and adults in both animals and humans. The present study has been conducted with the purpose of isolation and optimal PURIFICATION of Lactoferrin from cow’s milk.Materials and methods: Bovine colostrum was collected during 72 hours of delivery. First, milk fat was separated. To Isolate Lactoferrin from the rest of the milk proteins, the isolation process was conducted in two steps. Casein was precipitated using ammonium sulfate and in the next step Lactoferrin was isolated using CM-Sephadex-C50 cation exchange chromatography column with FPLC. To identify the isolated protein SDS-PAGE method was used.Results: The pure active protein, with a molecular weight of 80 kDa, with concentration of 2.4 mg/ml was obtained. The degree of PURIFICATION implementing after cation exchange chromatography column was 4 and PURIFICATION efficiency 90%.Conclusion: Considering the increase in the clinical and nutritional applications of Lactoferrin and particularly its immunomodulatory effects, finding an appropriate and efficient PURIFICATION method is very important. The results of the study show that the above-mentioned method, apart from simplicity and speed, can result in isolation of highly pure Lactoferrin.

Food allergy is responsible for most frequent allergic reactions in children under one year of age. Diagnostic tests such as skin test or specific IgE assay commonly need highly purified preparations of allergenic proteins. The aim of the present work was to purify three main proteins; casein, alpha-lactalbumin and beta-lactoglobulin allergenic extracts. First, casein was isolated by isoelectric precipitation of skimmed fresh milk serum or whey. PURIFICATION of alpha-lactalbumin was based on fractionittion of whey proteins by ammonium sulphate and gel filtration on a Sephadex G-50 column. Beta-lactoglobulin was purified by polyethylene glycol fractionation of whey proteins and ion exchange chromatography on a DEAE-Sepharose column. The isolated proteins were analyzed by polyacrylamide gel from fresh skimmed milk by hydrochloric acid were more soluble in weak alkaline water and purer than the other preparations. Purity of extracts in SDS-PAGE was estimated 95 percent. SDS-PAGE result of isolated alpha-lactalbumin and beta-lactoglobulin and reaction of these products with specific antibodies produced in immunized rabbits showed that they are highly pure. Electrophoretic pattern of purified alpha-lactalbumin or beta-lactoglobulin were composed of a -Singleband, in 14 or 18 KD respectively. In the present investigation three major milk proteins were highly purified. These products can be used in specific tests, i.e. skin test or ELISA.

The application rate of increase in demand for hydrogen and hydrogen-hydrogen separation by membranes has been investigated in this study. Hydrogen by distillation, refrigeration, pressure swing adsorption and membrane separation can be. The method of separating hydrogen, the membrane is the best way - is. Palladium and palladium alloy membranes for hydrogen separation using are very good. The use of composite membranes increases the penetration rate in India. In these membranes, the diffusion rate of hydrogen through the hydrogen affects and the results show that the rate of hydrogen through the metal film is to support more support to the metal film.

In this study Escherichia coli DE3 containing expression vector (pET21a) with cloned Persian sturgeon growth hormone (psGH) gene was grown in 10 mL LB broth on a 150 rpm shaker, at the temperature of 37oC. At the late log phase (determined by OD standard curve) 100 mL isopropyl b-D-1-thiogalactopyranoside (IPTG) was added for induction of GH synthesis. Samples were taken every 2 hours and after bacterial cells lysis crude extracts with recombinant proteins inclusion bodies (IB) were loaded on 15% SDS-PAGE gel. Thenafter staining, comparative concentrations of rpsGH were measured by densitometric scanning of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) gel it was more than 90 %. The maximum yield of GH was observed after 4 hours of growth. To recover active psGH from inclusion bodies we used imidozole to obtain most of the total recombinant protein in the soluble fraction. PURIFICATION of 6xhisN tag recombinant psGH has been performed using affinity chromatography where nickel was bound to an agarose bead by chelation using NTA (nitrilotriacetic acid) beads. The overall yield of the purified monomeric psGH was approximately 50% of the initial IB proteins. The PURIFICATION manipulations including IB isolation and solubilisation, protein refolding by dialyze and affinity chromatography ensure yields of biologically active psGH up to 30%. This study shows that, the affinity chromatography is a powerful and very specific method for recombinant proteins PURIFICATION of psGH.

Background: Brucellosis is still considered as one of the major zoonosis afflicting Syrian health and economy. This disease is caused by members of the genus Brucella which are gram-negative bacteria living facultatively within mammalian cells during infection. Objectives: In this paper, a strategy was developed to introduce a new generation of binders called Nanobodies (Nbs) in our combat against Brucella. Nbs are genetically engineered camelid-derived single-domain antibody fragments that are very stable and highly soluble, making them promising tools in numerous biotechnological and medical applications. Materials and Methods: In our previous work, three Nb-displaying phages (Nb-phage), referred to as NbBruc01, 02 and 03, were retrieved by a phage display panning of a Nb library constructed from Brucella- immunized camel. In this work, soluble Nbs were produced after recloning their genes in protein expression plasmid followed by PURIFICATION with affinity chromatography. Results: Interestingly, two of these soluble Nbs (NbBruc02 and 03) were able to detect Brucella antigens from two main Brucella species (B. abortus and B. melitensis) and distinguish them from those of Yersinia. This is remarkable as the camel IgG failed in such antigen discriminations. High similarity, mainly in the structure of lipopolysaccharides (LPS) of these different types of bacteria, causes regular serum cross reactivity and thus lack of specificity urging the need for more accurate diagnostic techniques, e.g. a multiplex PCR. Furthermore, NbBruc02 and 03 targets may represent Brucella immunodominant proteins as shown by immunoblotting. Conclusions: In addition to their own importance, identifying these antigenic targets will open new perspectives for diagnosis, vaccines and treatment of Brucellosis.

This paper demonstrates technique of water PURIFICATION using electro-coagulation method. This system is composed of DC electric source 200 V 30 A connect to the anode and cathode terminals. The DC power supply can be received from utility or solar energy. The sample of raw water from reservoir is used to conduct experimental reaction with electrocoagulation system in order to improve water quality. The water PURIFICATION experimental was implemented by batch processing with varying electrolysis time. The parameter of electro-coagulation and water quality parameters are collected such as electric voltage, electric current, water temperature, pH, dissolved oxygen (DO), total dissolved solid (TDS) and electro-conductivity. The result found that the water quality has improved with the standard of domestic water supply and also drinking water standard.

Background and Purpose: It is thought that transplantation of islet cells would cure diabetic patients in world. Islet cells transplantation in people suffering from diabetes is of technical interest. A standardized procedure was developed for the preparation of rat islet cell grafts for PURIFICATION of islet cells.Materials and methods: In this process, after collagens digestion of pancreases, islets were isolated and dissociated, then with enzymatic procedure by DNase and trypsin, the islet cells changed in to single cells and these cells were assayed by flow cytometery. Results: Flow cytometery of these cells indicated that there were 91% of beta cells in cell suspension. Most of the exocrine particles were lost during digestion.Conclusion: Purified endocrine islet cell grafts were prepared by pure beta-cells, with or without endocrine non-beta cells. The purified aggregates were devoid of non-endocrine cells and damaged cells.