A CATALASE FROM STREPTOMYCES-COELICOLOR A3(2)

Catalase was purified from the Cram-positive bacterium Streptomyces co elicolor A3(2) in a three-step purification procedure comprising (NH4) (2)SO4, fractionation, Phenyl-Sepharose chromatography and Mono Q chro matography. The purification of catalase, as judged by the final speci fic activity of 110000 U mg(-1), was 250-fold with a 35% yield. The na tive protein was a homotetramer with a subunit M(r) 55000. N-terminal and internal peptide sequence analyses showed that there was a high de gree of sequence similarity between the S. coelicolor catalase and oth er 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 inves tigated and elevated catalase activity was found in stationary-phase c ells.