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Electronic Journal of Biotechnology ISSN: 0717-3458
  © 2011 by Universidad Católica de Valparaíso -- Chile
Vol. 14 No. 3, Issue of May 15, 2011
 


Fig. 3 Purification of rSLLyz by reversed-phase chromatography. (a) On-column refolding of the thrombin treated GST fused rSLLyz and purification of the cleaved rSLLyz. , antibacterial activity detected by inhibition zone assay; , absorbance at 206 nm; and, acetonitrile concentration. (b) SDS-PAGE analysis of the bio-active recombinant peak in Figure 3a. M, protein marker; lane 1, 1 μg of the bio-active recombinant; lane 2; 3 μg of the bio-active recombinant; lane 3, 1 μg of the native S. litura lysozyme from hemolymph (nSLLyz). (c) Purification of rSLLyz from the bio-active protein. , antibacterial activity detected by inhibition zone assay; , absorbance at 206 nm; and , acetonitrile concentration. (d) SDS-PAGE analysis of the bio-active recombinant peak in Figure 3c. M, protein marker; lane 1, 1 μg of the bio-active recombinant in Figure 3c; lane 2, 1 μg of nSLLyz. (e) Inhibition zone assay analysis of 1 μg of rSLLyz, 1 μg of nSLLyz, and 3 μl of 0.05% TFA were loaded.