@article{mbs:/content/journal/micro/10.1099/00221287-129-12-3549, author = "Lu, Wei-Ping and Kelly, D. P.", title = "Purification and Some Properties of Two Principal Enzymes of the Thiosulphate-oxidizing Multi-enzyme System from Thiobacillus A2", journal= "Microbiology", year = "1983", volume = "129", number = "12", pages = "3549-3564", doi = "https://doi.org/10.1099/00221287-129-12-3549", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-129-12-3549", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "A soluble thiosulphate-oxidizing multi-enzyme system, precipitated from a crude cell extract of Thiobacillus A2 with ammonium sulphate, has been resolved into four essential components by DEAE-Sepharose chromatography, gel filtration of Sephadex G-100 and G-200, hydrophobic interaction chromatography on phenyl-Sepharose and preparative isoelectric focusing. Oxidation of thiosulphate to sulphate coupled to the reduction of horse-heart cytochrome c as electron acceptor was catalysed by two colourless proteins (enzyme A: M r, 16000; and enzyme B: M r, 64000). cytochrome c 552.5 (M r, 32000) and cytochrome c 551 (M r, 300000). Enzymes A and B were purified 110- and 280-fold, respectively. Sulphite: cytochrome c oxidoreductase was also purified 660-fold. The mechanism of action of the system is discussed.", }