A catalase from Streptomyces coelicolor A3(2).
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 110,000 U mg-1, was 250-fold with a 35% yield. The native protein was a homotetramer with a subunit M(r) 55,000. 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.
Walker
G E
GE
Departments of Biochemistry1 and Genetics2, University of Glasgow, Glasgow G12 8QQ, UK.
Dunbar
Bryan
B
Department of Molecular and Cell Biology, University of Aberdeen, Aberdeen AB9 1AS, UK.
Hunter
Iain S
IS
Department of Molecular and Cell Biology, University of Aberdeen, Aberdeen AB9 1AS, UK.
Nimmo
Hugh G
HG
Departments of Biochemistry1 and Genetics2, University of Glasgow, Glasgow G12 8QQ, UK.
Coggins
John R
JR
Departments of Biochemistry1 and Genetics2, University of Glasgow, Glasgow G12 8QQ, UK.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002374:Catalase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013302:Streptomyces / Q000201:enzymology*
D001426:Bacterial Proteins; D002374:Catalase