Expressing the divine revelations and religious precepts in an interesting and attractive form can greatly influence the way they are adopted by the human societies and lead them to salvation. However, the success of the sacred artist in performing such great task depends on his/her pure mind and imagination. As has been proved since the time of Socrates and Plato, the origin of art is imagination. This issue has also been discussed in details among Islamic philosophers. The founder of Mithal World in Islamic philosophy is Suhrevardi and later MullaSadra who elaborated on this issue. According to them, any symbol which arose in art is a symbol created in "the detached imagination" and offered by "the attached imagination" of the artist. Thus, depending on the artist's preoccupation, his imagination is trained and improved. In this paper, after a brief explanation about the nature of imagination (attached and detached), the role and stand of art from the perspective of Islamic philosophers has been discussed, then the relationship between the sacred arts and the purity of mind has been expressed in details.

Hepatitis B virus (HBV) is considered a global health problem whid. affects 360 millions of people worldwide and about two millions in Iran. Among HBV antigens, the physiological function of HBeAg is still unresolved. In this respect, its presence in positive patients is regarded as a marker of viral replication and it may have roles in pathogenesis and persistence of the disease, while no obvious changes in clinical course of the disease has been observed in negative patients. As a result, availability of this protein with characteristics of the naturally occurred antigen in high amounts and of the same purity is highly required for being. Utilized in medical research and diagnosis. At present, recombinant HBeAg is being produced in different expression systems for various applications. In the present study, by application of a simple expression/PURIFICATION system in E. coli and with the aim of producing physiologically natural HBeAg, that portion of the gene, which exactly corresponds to amino acid sequence of the blood-borne HBeAg have been isolated and cloned into pQE-30 vector which adds a 6x Histag to the N-terminal of the inserted gene, providing the ability of one step PURIFICATION method by exploiting Ni-NTA column chromatography. Following restriction analysis and confirmation of recombinant vector accuracy, transformation to E. coli M15 cells and IPTG-mediated induction for protein expression was performed. Analysis of the purified protein by SOS-PAGE, ELISA and Western blotting indicated that obtained recombinant HBeAg had the perfect antigenic properties of authentic HBeAg and addition of the His-tag segment which produces extra epitopes on this antigen had no adverse effect on these properties. The results of this study clearly describe a very simple and efficient system for providing recombinant HBeAg in high yield and purity for diagnostic and physiological research applications.

Tuberculosis remains as an important socioeconomical and medical problem throughout the world and especially in Iran. Early and timely diagnosis of pulmonary and extrapulmonary tuberculosis is vital to initiate prompt treatment. Current diagnostic methods are either slow or lack enough sensitivity or specificity. Several mycobacterial antigens are involved in the complex interaction with the immune system of the host. Their identification is important for both diagnosis and protection against mycobacteria.Antigen 60 (A60) is a thermostable antigen found in the cytosol of M. bovis and M. tuberculosis.An ELISA test using A60 is designed for diagnosis of tuberculosis with satisfactory results. In previous studies, A60 has also showed a protective effect against experimental infections and useful immunotherapeutic effects in promotion of cancer development. In the present work.we tried to purify A60 from the cytoplasm of BCG. A60 was purified by exclusion gel chromatography using sepharose 4B. A60 was recognized by bidimensional immunoelectrophoresis with anti-BCG and anti-A60 antiserum, where it appears as the less mobile component. In agarose electrophoresis, A60 showed only one band but in immunodiffusion it showed two immunoprecipitinogen lines with anti-BCGanti-serum.In analyzing with dot blotting, both cytoplasm and cell wall of BCG showed positive reaction with anti- A60 anti-serum. When A60 was fractionated by SDS-PAGE and analyzed by western blot using anti-A60 antibody,65,46,40,38 and 35 KDa protein fractions were identified. It is concluded that A60 is a macromolecularantigen of BCG with a molecular weight of 106-107 Da and is a lipoprotein-polysaccharide complex which contains several proteins. A60 is present in both cytoplasm and cell wall of BCG and can easily be purified from BCG vaccine using exclusion chromatography by sepharose 4B, to be used for designing diagnostic tests for TB.

Peroxidase ((PRO) (EC.1.11.1.7)) has applications in many diagnostic procedures such as ELISA and immunoperoxidase. Concerning HRP related products; we are dependent to other countries. Therefore the PURIFICATION of PRO can be an economically important object. Raphanus sativus Var Niggera was tested to be a suitable source for PRO PURIFICATION. The steps of PURIFICATION were included: extraction by phosphate buffer (0.05 M, pH 7), ethanol and ammonium sulfate precipitation and ion-exchange chromatography on DEAE-Cellulose. Based on the affinity to DEAE-Cellulose column a major alkalin form and one minor acidic form of PRO were detected. The fold of PURIFICATION was 102 and the recovery was 67%. The molecular weight and Rz for the alkalin isoenzyme were calculated to be 40000 daltons and 1.95, respectively. The extent of enzyme purity was verified by SDS-PAGE. Regarding the economical point of view, mass production of this enzyme as internal product is suggested.

Introduction: Oxalate oxidase (EC.1, 2, 3, 4), an acute phase protein of plants, is used widely in agriculture, food industries, medical diagnosis of kidney stones and oxaluria. In this study oxalate oxidase from barley was purified and partially characterized. Materials & Methods: Roots and sprouts of barley cultured in hydroponic states were separated and extracted. Ion exchange resins of the enzyme were done through heat treatment (80°C, 3min), ammonium sulphate fractionation and two-step chromatography. PURIFICATION and weight-determining of the enzyme were done by DEAE-Cellulose and DEAE-Sepharose fast flow, respectively. The enzyme activity was measured by spectrophotometric and specific gel staining methods. Purity and molecular mass of the product was estimated using SDS-PAGE. Isoelectric points (pIs) of the separated enzymes were estimated using chromatofocusing and isoelectric focusing. In addition, the effect of different concentrations of urea and denaturing agents were tested on the enzyme activity.  Results: Oxalate oxidase was purified at least 688-fold with purity of more than 90 percent. The molecular mass of the enzyme was estimated to be 25-26 and 115-120 KDa, respectively in reducing and non-reducing SDS-PAGE. The enzyme sub-units showed no activity in the specific gel staining method. At least two isoenzymes with pIs of 6.8 and 6-6.2 were identified. The purified enzyme was resistant to many denaturing agents such as heat, urea and detergents. These characteristics make oxalate oxidase a suitable enzyme for oxalate assays. Conclusion: So in accordance with the obtaind data from this study, it can be concluded that we can utilize the PURIFICATION method of this enzyme for measuring oxalate.

Background & Objectives: Clostridial neurotoxin inhibits neurotransmitter release by selective and specific intracellular proteolysis of synaptosomal associated protein of 25KDa (SNAP-25), synaptobrevin/VAMP-2 and syntaxin. SNAP-25 is one of the components that forms docking complex in synaptic ends. This protein is subtrate for botulinum neurotoxins types A, C, and E. Each of these toxin serotypes specifically cleaves SNAP-25 in a particular position and thereby blocks docking and synaptic vesicle membrane fusion and finally prevents neurotransmitter exocytosis and transition of neurotic signals. Recombinant production of SNAP-25 in the laboratory can be used as a subtrate for the detection of clostridium botulinum types A, and E neurotoxins.Materials & Methods: In order to use the protein as a subtrate for detection of different types of clostridium neurotoxins in-vitro the protein was produced by recombinant technique. The cDNA from SNAP-25 was synthesized from total RNA purified from frozen Rattus norvegicus brain and amplified by RT-PCR the amplified fragment was cloned into pET32a expression vector. The identity of recombinant protein was confirmed by Western blot using specific antibody and finally the recombinant protein was purified through an affinity column chromatography (Ni-NTA).Results: The optimum conditions of expression of SNAP-25 were found to be IPTG (1mM) and incubation at 37oc for 5 hours. The recombinant protein was isolated and purified using Ni-NTA column with imidazole at a concentration of 25OmM. Using enterokinase to cut the fision at 37oC comparatively yielded better results than room temperature.Conclusion: The protein retained its structure during the PURIFICATION process being suitable for cutting and further tests. The purified protein we obtained can be used as substrate for detection of clostridium botulinum types A, and E toxins.

The homeobox genes are known to play a crucial role in controlling the development of multicellular organisms. The majority of these genes have been determined to express regulatory proteins act as a regulatory protein. These transacting factors regulate the expression of proteins that are necessary during the developmental processes throughout the body. TGIFLX/Y is a homeobox gene and it contains two genes: TGIFLX (X-linked) and TGIFLY (Y-linked) are specifically expressed in human adult testes. TGIFLX has originated from retrotransposition of TGIF2, located on long arm of chromosome 20 (q11.2-12), onto the X chromosome. To date, the role of TGIFLX/Y are unknown, therefore, in order to get insight into the potential roles of TGIFLX, we cloned and produced the GSTTGIFLX fusion protein. The purified protein was recognized by anti-GST antibodies. Through a single PURIFICATION procedure using MagneGST beads, approximately 8 mg of the recombinant protein was obtained per liter from bacterial culture. The production of this recombinant protein will now permit the investigation of TGIFLX target genes as well as identification of co-factors or partner proteins involved in TGIFLX function in normal and abnormal development.

Background: Tetanus is a kind of neurological disease characterized by rigidity and spasm of muscles. The causative agent of this fatal disease is known as Tetanus Toxin, Clostridium tetani. The Tet-anospasmin consists of three chains: HN, HC and L. The HC chain is binds domain and immunogenic part of toxin, so it is proposed as a vaccine candidate. In this study, the recombinant HC protein obtained from synthetic HC gene was investigated for its immunogenicity. Additionally, antiserum and polyclonal antibody was prepared against this agent.Materials and Methods: Recombinant His-tagged Hc protein was expressed in Escherichia coli Bl21 DE3 and purified with Ni-NTA column. Then, rHc protein was used for animal immunization. Along with survey of antibody titer, serum polyclonal antibody was purified by G column.Results: After gene optimization, expression and PURIFICATION, rHC protein was confirmed by western blot technique. Immunization of mice showed high titer of antibody against recombinant protein. An-tibody PURIFICATION from immunized animal serum was carried out as well.Conclusion: The recombinant HC protein production and its immunogenicity investigation showed high titer of antibody against Tet-anospasmin.