Enzymic properties of the neo-plasmin-Val-442 (miniplasmin)
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The X-ray Crystal Structure of Full-Length Human Plasminogen
2012, Cell ReportsCitation Excerpt :Indeed, this disulphide is broken in molecule B, possibly as a consequence of exposure of the crystals to synchrotron radiation. These data, however, provide an explanation for the observed susceptibility of KR5 to disulphide reduction by phosphoglycerate kinase (Lay et al., 2000) as well as the cleavage events that take place within this domain during the production of the potent angiogenic factor angiostatin (KR1-4) and miniplasmin (KR5-SP) (Christensen et al., 1979). To conclude, we suggest that KR1 and KR5 in the closed plasminogen govern the proenzyme recruitment and initiation of conformational change, respectively.
Refolding, purification, and activation of miniplasminogen and microplasminogen isolated from E. coli inclusion bodies
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