Rapid purification of two thermophilic proteinases using dye-ligand chromatography.
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.
Cowan
D A
DA
Thermophile Research Unit, University of Waikato, hamilton, New Zealand.
Daniel
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RM
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
D002021:Buffers; D004396:Coloring Agents; D008024:Ligands; D014227:Triazines; C026268:procion green H-E4BD; D012685:Sepharose; D010450:Endopeptidases