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 scalable 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*; D001665:Binding Sites; D002021:Buffers; D002846:Chromatography, Affinity / Q000379:methods*; D004396:Coloring Agents; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D008024:Ligands; D012685:Sepharose; D013824:Thermus / Q000201:enzymology*; D014227:Triazines
chemical_list: D002021:Buffers; D004396:Coloring Agents; D008024:Ligands; D014227:Triazines; C026268:procion green H-E4BD; D012685:Sepharose; D010450:Endopeptidases