Publications by authors named "Chinnathambi Thangadurai"

High throughput expression of proteins is often hampered by the failure of certain proteins to express in the particular host strain used for the study. The identification of a host strain compatible for a wide variety of proteins is desirable. In this study, the recombinant expression of therapeutic proteins Erythropoietin (EPO), Streptokinase (SK) and Tumor Necrosis Factor Receptor Extra cellular domain (TNFR ED) that vary widely in their chemical nature was studied in four different strains of namely BL21 (DE3), BL21 (DE3) pLys S, BL21 (DE3) Rosetta pLys S and GJ1158.

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Streptokinase (SK) is a thrombolytic agent that is widely used to treat myocardial infarction and pulmonary embolism. The lack of fibrin specificity of SK for the clot lysis is one of the limitations of SK. In this study, we have incorporated the finger and Kringle 2 domains from the human tissue type plasminogen activator gene (t-PA) at the 5' end of the SK gene.

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Rare codons and their effects in heterologous protein expression in Escherichia coli were addressed by many investigators. Here, we propose that not all rare codons of a foreign gene have negative effect but selective codon among them and its specific position in the downstream of the start codon modulates the expression. In our study, streptokinase (47 kDa), encoded by skc gene of Streptococcus equisimilis was expressed in E.

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In situ activity assay is one of the promising techniques for the characterization of peptide antibiotics. This assay was carried out for the peptide purified from a new bacterial isolate Paenibacillus alvei and commercial peptide antibiotic polymixin E. Towards this, the routine and new protocols were tried.

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