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Rapid purification of two thermophilic proteinases using dye-ligand chromatography.

作者信息

Cowan D A, Daniel R M

机构信息

Thermophile Research Unit, University of Waikato, hamilton, New Zealand.

出版信息

J Biochem Biophys Methods. 1996 Apr;32(1):1-6. doi: 10.1016/0165-022x(95)00024-l.

DOI:10.1016/0165-022x(95)00024-l
PMID:8773542
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.

摘要

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