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dc.contributor.authorCowan, Don A.
dc.contributor.authorDaniel, Roy M.
dc.date.accessioned2010-08-30T03:18:04Z
dc.date.available2010-08-30T03:18:04Z
dc.date.issued1996
dc.identifier.citationCowan, D.A. & Daniel, R.M. (1996). Rapid purification of two thermophilic proteinases using dye-ligand chromatography. Journal of Biochemical and Biophysical Methods, 31(1-2), 31-37.en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4468
dc.description.abstractDye-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 l volume.en_NZ
dc.language.isoen
dc.publisherElsevieren_NZ
dc.subjectthermophilicen_NZ
dc.titleRapid purification of two thermophilic proteinases using dye-ligand chromatographyen_NZ
dc.typeJournal Articleen_NZ
dc.identifier.doi10.1016/0165-022X(95)00028-Pen_NZ


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