In order to achieve high quality crystals, it is necessary to purify the raw material. In the present experimental study, the zone melting method was used to purify Lithium Flouride powder. A small amount of melt moves slowly from the solid area in order to remove impurities in the frozen solid. In this case, the number, size and length of the zone melting affect the final result, and cause the optimal distribution of solutes. At the beginning, the regional PURIFICATION system was equipped. The mechanism of work was moving furnace on a graphic crucible with full of LiF powder by 20 mm/h-1. This procedure was followed in a vacuum for 7, 9 and 14 times. At last the amounts of impurities such as Fe, Ba were measured by ICP (Inductively Coupled Plasma) analysis before and after PURIFICATION.

BACKGROUND AND OBJECTIVE: Ferritin with molecular weight of 450 kDa is the most important iron storage protein and is made of 24 subunits consisting of light and heavy chains. Each ferritin molecule is able to store 4500 Fe3+ molecules. The aim of this study was to determine the preparation of highly pure ferritin for usage in diagnostic and research systems. METHODS: In this study, ferritin was extracted and purified by homogenizing liver tissue, heating at 75 degrees centigrade, ammonium sulfate fractionation and gel filtration chromatography on sephadex G-200 column. The purify of ferritin was improved by using recycling chromatography. Resulted protein was electrophoreses on polyacrylamide gel in the presence of sodium dodecylsulfate (SDS-PAGE). Existence of ferritin was confirmed by ELISA test and potassium ferricyanide staining of gel. Silver nitrate staining of gel was used to confirm the purity of ferritin. Electrophoresis of ferritin under reducing conditions in presence of 2- mercapto ethanol was done to show the subunits (19 and 21 kDa) of ferritin. FINDINGS: This PURIFICATION method resulted in very pure ferritin and the yield was 100 µg/gr of wet liver tissue. Electrophoresis of ferritin under reducing conditions in presence of 2- mercapto ethanol showed the both subunits (19 and 21 kDa) of ferritin.CONCLUSION: Highly pure ferritin resulted by this method is appropriate for diagnostic and research purpose and the yield is reasonable comparing other studies.

As the Kor river water is applied for agricultural uses in Fars province and also urban, agricultural and industrial wastewater are poured to it, a study was carried out on variation of dissolved oxygen concentration and water quality parameters along the Kor river, from Band-e Amir to the Bakhtegan lake (specially in critical time) . Industrial pollution sources are located up the Band-e Air and also urban and agricultural pollutants are poured to the river through the Ahoochar drain. Therefore, 11 sampling stations were selected down the band-e Amir. Most of the selected stations are located in diversion barrages established for agricultural uses. In each station, two samples were taken for determination of dissolved oxygen, one sample for measurement of biochemical oxygen demand for seven days (BOD7) and the other for some parameters such as TDS, PH,… Then, dissolved oxygen content and its variation along the distance were studied and also effective factors in decrease and in create of it were calculated by means of Qualkor model which was compiled in visual basic. Results of such experiments are the presentation of oxygen sag curve which is applied for the Kor river in two separate situations (critical condition and under study condition). In this study, dissolved oxygen content along the distance was not decreased from 4 mg/L (standard Limit for aquatics), but in critical conditions, this amount was less than standard limit in all the stations except in the first station. Dissolved oxygen content reached zero between the stations 2 and 4, so aquatic life is confronted in danger.

Alkaline phosphatase, an orthophosphoric monoester phosphohydrolase Ec 3.1. 3.1., is a glycoprotein dimer. It is active in alkaline PH and needs mg2+ ion as an activator. This membrane-bound enzyme is widely distributed in nature. In this study, it was purified from human placenta in seven steps. Placenta was homogenated and the enzyme was extracted through following steps: Butanol extraction, filtration on sephadex G200, ammonium sulfate precipitation, aceton precipation and DEAE cellulose chromatography with a gradient of sodium chloride. A peak of the enzyme activity at sodium chloride concentrations of 0.087 to 0.093 mg was observed on DEAE cellulose chromatography. The specific activity of the enzyme and PURIFICATION factor were observed to be 209.9 U/mg and 611.8 respectively. At the final steps of preparative electrophoresis, the purified enzyme was. subjected to polyacrylamide disc gel electrophoresis. P-nitrophenyl phosphate was used, instead of N-naphthyl phosphate, to stain alkaline phosphatase. The appearance of a yellaw band proved the PURIFICATION of the enzyme.

Chitinases are widely distributed in nature and play important roles in degradation of chitin. Chitin, a linear polymer of N-acetylglucosamine residues, has been the most abundant polymer in nature after cellulose. It plays a major role in fungal cell walls. Chitinase enzymes degrade the chitin polymer into its component residues by breaking the b-1,4 glycosidic bonds. As a producer of a variety of chitinase enzymes, the filamentous fungus, Trichoderma sp., has become an important means of biological control for fungal diseases.The aim of this study was to identify a Trichoderma sp. isolate with over production of chitinase. Trichoderma atroviride PTCC5220 was selected as over producer of chitinase enzyme among 31 different isolates of Trichoderma sp. Also chitinase 42 kDa (Chit42) was purified from supernatants of T. atroviride grown in medium supplemented with colloidal chitin as the sole carbon source. Enzyme PURIFICATION was achived in two steps ion exchange chromatography using CM-Sepharose and DEAESepharose. Elution of the column was carried out with 1 M NaCl gradient. The purity of chit42 was investigated by SDS-PAGE. The results showed one band about 42 kDa after the second step of chromatography. The purified protein showed chitinase activity in enzyme assay technique.

The histone-like protein HU is the most-abundant DNA-binding protein in bacteria.The HU protein non-specifically binds and bends DNA as a hetero- or homodimer, and can participate in DNA supercoiling and DNA condensation. It also takes part in DNA functions such as replication, recombination, and repair. HU does not recognize any specific sequences but shows a certain degree of specificity to cruciform DNA and repair intermediates such as nick, gap, bulge, etc. To understand the features of HU binding to DNA and repair intermediates, a fast and easy HU protein PURIFICATION method is required. Here we report a two-step PURIFICATION procedure of HU from Halobacillus karajensis (the gram positive and moderately halophilic bacteria isolated from Karaj surface soil). The method of HU PURIFICATION allows obtaining a pure nontagged protein. Salting out and ion exchange chromatography were applied for PURIFICATION, and the purified protein was identified by immunoblotting. Results showed that the molecular weight of the purified protein was approximately 11 kDa which is immunologically similar to the Bacillus subtilis HU protein (HBsu).

Helicobacter pylori are the most important cause of chronic stomach infection, chronic gastritis, peptic ulcers and gastric cancer in men. This gram-negative microorganism is S-shaped, microaerophillic and has potent urease activity. After H. pylori ingestion, the microorganism attaches to the epithelial surface of stomach and is clonized. Subsequently, the physiologic and cytological damage is occurred. In the present work stomach biopsies were prepared by an experienced endoscopist physician, inoculated in transport media and sent to laboratory. Concurrently, 5ml blood sample was   obtained from patients. Biopsy sample was homogenized in an aerobic sterile condition and then was cultured on selective media for 5 to 7 days at 37°C the pure colonies were harvested from media and preserved in PBS sterile solution, then, samples subjected to ultrasound waves that caused bacteriallysis.12.5% SDS-PAGE using wide range molecular weight marker was done. Lysed bacteria were divided to pure protein fractions by Gel filtration chromatography. Samples were quantified by spectrophotometer. Samples with high absorbance were incubated with positive sera and result was analyzed in regard to positive response in dot-blotting method. Antigenic profile of lysed bacterial electrophoresis indicates protein precipitation in 21, 8 kilo Dalton area. These results indicate the ability of antigens in stimulating immune response. Also in negative samples, a lower antibody response was seen. Therefore intact bacteria are not suitable for serological diagnosis and only specific proteins should be used for this purpose.      

Because of the importance of biomolecule extraction and its genetic investigations in the medical and forensic field with all the limitations such as sensitivity, nature of work, high cost, the need for highly skilled technicians, automation and portability of the system in terms of detection with existing technologies, several need not fulfilled. There is a need to integrate sample preparation and detection methods. To overcome these limitations, nowadays most studies have focused on improving detection technologies, and accordingly, advances in detection technologies microfluidics is one of the best systems with convincing feautures. Other advantages of this technology including the extraction of DNA and protein which is involved automation in a sample preparation, the ability to operate in small sample sizes as well as minimizing the consumption, cost, and processing time of solvents.

In order to gene cloning, at first desired gene should separate from other contaminants (proteins, primer-dimer bands unskilled, etc. ). Various physical and chemical methods were used for PURIFICATION of target gene from other contaminates; Here we have applied a new physical methods for PURIFICATION of gen from agarose gel under an electric field containing TAE. 1X fluid. We isolated PqHMGR form Panax quinquefoliusby using specific primers based on cDNA sequences. Ligation of isolated gene tovector and its cloning was done through E. coli (DH5α ). Finally, PqHMGR gene was purified by the foresaid device and after cloning in desired vector, extracted plasmid were sequenced for confirmation of gene PURIFICATION and cloning. Our resultd showed accuracy of this device in gene PURIFICATION.