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Articles by A.H. Salmanian
Total Records ( 2 ) for A.H. Salmanian
  H. Abtahi , A.H. Salmanian , S. Rafati , G.B. Nejad , M. Saffari , A. Ghazavi and G. Mosayebi
  This study was evaluated the ability of DNA vaccine encoding L7/L12 protein of Brucella sp. to induce cellular and humoral immune responses in BALB/c mice and the profile of cytokines and IgG sub classes were determined. Intra muscular vaccination of mice using L7/L12 gene. Three vaccinations at 3 week intervals were performed. Cytokines and IgG subclasses were analyzed 3 week after the last DNA vaccination. Splenic lymphocytes from L7/L12pCDNA3-vaccinated mice produced high levels of IFNγ (3100 pg mL-1) and low levels of IL-5 (300 pg mL-1), 3 weeks post-vaccination. The L7/L12pCDNA3 immunizations elicited high IgG2a isotype response in mice immunized. This antigen also induced IgG1 titers which were slightly lower than the IgG2a titers. Immunological analysis shows the appropriate immune response in BALB/c mice model after vaccination with L7/L12 gene. The high level of IFNγ and low level of IL-5 in combination with high IgG2a/ IgG1 ratio show the activation of Th1 cell response. The lower bacterial cfu from vaccinated mice in comparison with control groups show the efficiency of L7/L12 DNA vaccination in mice model.
  S. Mahmoudi , H. Abtahi , A. Bahador , G. Mosayebi and A.H. Salmanian
  Streptokinase (SK) is a potent plasminogen activator with widespread clinical use as a thrombolytic agent. In this study, we produce high level expression of recombinant streptokinase in E. coli by expression vector pET32a. Genomic DNA of streptokinase gene (SKC) was extracted, then amplified by polymerase chain reaction (PCR) method and sub-cloned to prokaryotic expression vector pET32a. Escherichia coli BL21 (DE3) pLysS were transformed with pET32a-skc and gene expression was induced by IPTG. The expressed protein was purified by affinity chromatography by Ni-NTA resin. High concentration of the recombinant protein obtained from the single-step purification by affinity-chromatography (Ni-NTA). The yield of recombinant streptokinase was nearly 470 mg L-1 of initial culture. Our data showed that production of recombinant streptokinase improved by pET32a in Escherichia coli.
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