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Articles by S. Mahmoudi
Total Records ( 2 ) for S. Mahmoudi
  F. Rajabzadeh , E. Pazira , M.H. Mahdian , S. Mahmoudi and M. Heidarizadeh
  The objective of this study was to study the desalination and desodification of sugarcane fields in Khuzestan plain. Leaching experiments were conducted on seven sites and intermittent ponding method was implemented for an applied water depth of 100 cm. Among four models fitted to desalinization and desodification estimations, an exponential model with a correlation coefficient of 0.735 and significance level at 1% was selected. In the second model, initial, final and equilibrium salinity, leaching efficiency and moisture content were considered and the fitted exponential model with R2 = 0.758 was determined as the best desodification. A simulation model called leaching process was developed to determine the amount of water and time needed for reclamation of the whole soils of the study area. Two scenarios were presented: scenario I contained initial leaching, barely cultivation and leaving plant residual during warm seasons, scenario II proposed initial leaching and heavy disk operation and then a pre-irrigation operation. Considering lowering consumed water depth for the soil reclamation and also higher yield in the first scenario, scenario I was selected as a best choice.
  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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