title: A single step purification for autolytic zinc proteinases.
abstract: We describe a novel single-step method for the purification of stromelysin-1 catalytic domain (SCD) via immobilized metal affinity chromatography under denaturing conditions that inhibit proteolytic activity followed by on-column refolding and spontaneous autolysis of the fusion peptide to yield pure, active stromelysin-1 catalytic domain. The methodology provides a general approach for the rapid purification of large quantities of zinc proteinases.
authors: Department of Chemistry, Duke University, LSRC B120, Durham, NC 27708, United States.
authors: Erin M
authors: EM
authors: Wilfong
authors: Ursala
authors: U
authors: Locklear
authors: Eric J
authors: EJ
authors: Toone
mesh_terms: D001329:Autolysis; D020134:Catalytic Domain; D002846:Chromatography, Affinity; D006639:Histidine / Q000737:chemistry; D007093:Imidazoles / Q000737:chemistry; D019278:Matrix Metalloproteinase 3 / Q000302:isolation & purification*; D009842:Oligopeptides / Q000737:chemistry; D017510:Protein Folding
chemical_list: C471213:His-His-His-His-His-His; D007093:Imidazoles; D009842:Oligopeptides; D006639:Histidine; D019278:Matrix Metalloproteinase 3; C005954:imidazoleacetic acid