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pubmed-article:19214390pubmed:abstractTextStaphylokinase (SAK) is a promising thrombolytic agent for treating blood-clotting disorders. Recombinant SAK (rSAK) was produced after integration of the gene into Pichia pastoris genome. The recombinant Pichia carrying multiple insertions of the SAK gene yielded high-level (approximately 1 g/l) of extracellular glycosylated rSAK (approximately 18 kDa) with negligible plasminogen activation activity. Addition of tunicamycin during the induction phase resulted in expression of non-glycosylated and highly active rSAK (approximately 15 kDa) from the same clone. Two simple steps of ion-exchange chromatography produced an homogenous rSAK of >95% purity which suitable for future structural and functional studies.lld:pubmed
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pubmed-article:19214390pubmed:year2009lld:pubmed
pubmed-article:19214390pubmed:articleTitleHigh-level expression of non-glycosylated and active staphylokinase from Pichia pastoris.lld:pubmed
pubmed-article:19214390pubmed:affiliationBiotechnology R & D, Lupin Limited, 46A/47A, Nande Village, Mulshi Taluka, Pune 411042, India.lld:pubmed
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