Abstract
Two enzymes containing thiosulfate sulfur transferase activity were purified fromChlorobium vibrioforme f.thiosulfatophilum by ion exchange chromatography, gel filtration and isoelectrofocusing. Enzyme I is a basic protein with an isoelectric point at pH 9.2 and has a molecular weight of 39,000. TheK m-values for thiosulfate and cyanide of the purified basic protein were 0.25 mM (thiosulfate) and 5 mM (cyanide). Enzyme II is an acidic protein. The enzyme has an isoelectric point at pH 4.6–4.7 and a molecular weight of 34,000. TheK m-values of the acidic protein were found to be 5 mM for thiosulfate and 125 mM for cyanide.
In addition to thiosulfate sulfur transferase activity, cellfree extracts ofChlorobium vibrioforme f.thiosulfatophilum also contained low thiosulfate oxidase activity and negligible thiosulfate reductase activity. The percent distribution of thiosulfate sulfur transferase and thiosulfate oxidase activities in the organism was independent of the offered sulfur compound (thiosulfate, sulfide or both) in the medium.
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Abbreviations
- C:
-
Chlorobium
- SDS:
-
sodium dodecylsulfate
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Dedicated to Prof. Dr. Norbert Pfennig on the occasion of his 60th birthday
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Steinmetz, M.A., Fischer, U. Thiosulfate sulfur transferases (Rhodaneses) ofChlorobium vibrioforme f.thiosulfatophilum . Arch. Microbiol. 142, 253–258 (1985). https://doi.org/10.1007/BF00693399
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DOI: https://doi.org/10.1007/BF00693399