RAPID PURIFICATION OF 2 THERMOPHILIC PROTEINASES USING DYE-LIGAND CHROMATOGRAPHY

Authors
COWAN DA DANIEL RM
Citation
Da. Cowan et Rm. Daniel, RAPID PURIFICATION OF 2 THERMOPHILIC PROTEINASES USING DYE-LIGAND CHROMATOGRAPHY, Journal of biochemical and biophysical methods, 32(1), 1996, pp. 1-6
Citations number
20
Categorie Soggetti
Biology,Biophysics,"Biochemical Research Methods
Journal title
Journal of biochemical and biophysical methods → ACNP
ISSN journal
0165022X
Volume
32
Issue
1
Year of publication
1996
Pages
1 - 6
Database
ISI
SICI code
0165-022X(1996)32:1<1:RPO2TP>2.0.ZU;2-T
Abstract
Dye-ligand chromatography has been used successfully for the purificat ion of extracellular thermostable proteinases from thermophilic Bacill us and Thermus cultures. Single-step purification factors of up to 115 -fold (for Thermus protease) and 2195-fold (for Bacillus protease) wer e obtained, Elution studies suggested that the mode of binding involve d the enzyme active sites. The method was readily scalable to 600 1 vo lume.