title: Rapid purification of two thermophilic proteinases using dye-ligand chromatography.
abstract: Dye-ligand chromatography has been used successfully for the purification of extracellular thermostable proteinases from thermophilic Bacillus and Thermus cultures. Single step purification factors of up to 115-fold (for Thermus protease) and 2195-fold (for Bacillus protease) were obtained. Elution studies suggested that the mode of binding involved the enzyme active sites. The method was readily scaleable to 600 1 volume.
authors.affiliation: Thermophile Research Unit, University of Waikato, Hamilton, New Zealand.
authors.forename: D A
authors.initials: DA
authors.lastname: Cowan
authors.forename: R M
authors.initials: RM
authors.lastname: Daniel
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002845:Chromatography / Q000379:methods; D004396:Coloring Agents; D010450:Endopeptidases / Q000302:isolation & purification*; D008024:Ligands; D013824:Thermus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D004396:Coloring Agents; D008024:Ligands; D010450:Endopeptidases