A catalase from Streptomyces coelicolor A3(2)

Walker, G.E., Dunbar, B., Hunter, I. S., Nimmo, H. G. and Coggins, J. R. (1995) A catalase from Streptomyces coelicolor A3(2). Microbiology, 141(6), pp. 1377-1383. (doi: 10.1099/13500872-141-6-1377) (PMID:7670639)

Abstract

Catalase was purified from the Gram-positive bacterium Streptomyces coelicolor A3(2) in a three-step purification procedure comprising (NH4)2SO4, fractionation, Phenyl-Sepharose chromatography and Mono Q chromatography. The purification of catalase, as judged by the final specific activity of 110000 U mg-1 was 250-fold with a 35% yield. The native protein was a homotetramer with a subunit M r 55000. N-terminal and internal peptide sequence analyses showed that there was a high degree of sequence similarity between the S. coelicolor catalase and other microbial and mammalian catalases. Southern blot analysis indicated that there was a single catalase gene in S. coelicolor. The specific activity of catalase throughout the growth of batch cultures was investigated and elevated catalase activity was found in stationary-phase cells.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Nimmo, Professor Hugh and Coggins, Professor John
• Authors: Walker, G.E., Dunbar, B., Hunter, I. S., Nimmo, H. G., and Coggins, J. R.
• College/School: College of Medical Veterinary and Life Sciences > School of Molecular Biosciences; College of Medical Veterinary and Life Sciences > School of Life Sciences
• Journal Name: Microbiology
• Publisher: Microbiology Society
• ISSN: 1350-0872
• ISSN (Online): 1465-2080