Biochemical characterization of the catalytic domain of human matrix metalloproteinase

HIGHLIGHTS

• who: Jan O. Stracke from the main, was produced, thereby altering E P/P V and C S by ligating the PstI and NcoI fragment from pro⌬, MMP-19(E P/ P V) into the pRSET B vector containing the mutation for C S in the catalytic domain, previously cleaved with the same restriction enzymesExpression and refolding were performed as described above. All expression vectors were sequenced using the dideoxy chain termination method and confirmed the correct sequence for each construct. Expression and Purification of Full-length , Human , was purified from culture medium conditioned by , mouse myeloma . . .
  

   

  

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