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Figure 1 | BMC Molecular Biology

Figure 1

From: Characterization of a novel bifunctional mutant of staphylokinase with platelet-targeted thrombolysis and antiplatelet aggregation activities

Figure 1

Production of an engineered staphylokinase-based RGD-SAK. (A) Amino acid residues and nucleotide sequences of SAK and RGD-SAK are shown. The lys35 has been substituted with Arg to constitute a RGD motif and sequence analysis confirmed the successful mutagenesis. (B) Coomassie blue-stained 15% SDS-PAGE showing expression of RGD-SAK. Lane M, protein marker; lanes 1–6, induced for 0, 0.5, 1, 1.5, 2, 2.5 h. (C) Purification of recombinant protein RGD-SAK. Lane M, protein marker; lane 1, cytosol fractions; lane 2, purification after SP-Sepharose; lane 3, purification after Sephadex G-50; lane 4, purification after Q-Sepharose. (D) Western blot analysis with polyclonal anti-SAK antibodies.

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BMC Molecular Biology

ISSN: 1471-2199

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