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Journal Abstract Search
87 related items for PubMed ID: 4824902
1. Reduction of sulphite to sulphide catalysed by desulfoviridin from Desulfovibrio gigas. Jones HE, Skyring GW. Aust J Biol Sci; 1974 Feb; 27(1):7-14. PubMed ID: 4824902 [No Abstract] [Full Text] [Related]
2. Purification of the enzyme reducing bisulfite to trithionate from Desulfovibrio gigas and its identification as desulfoviridin. Lee JP, Peck HD. Biochem Biophys Res Commun; 1971 Nov 05; 45(3):583-9. PubMed ID: 5128167 [No Abstract] [Full Text] [Related]
3. Effect of enzymic assay conditions on sulfite reduction catalysed by desulfoviridin from Desulfovibrio gigas. Jones HE, Skyring GW. Biochim Biophys Acta; 1975 Jan 23; 377(1):52-60. PubMed ID: 235295 [Abstract] [Full Text] [Related]
6. Isolation of assimilatroy- and dissimilatory-type sulfite reductases from Desulfovibrio vulgaris. Lee JP, LeGall J, Peck HD. J Bacteriol; 1973 Aug 23; 115(2):529-42. PubMed ID: 4725615 [Abstract] [Full Text] [Related]
7. A method for the electrophoretic characterization of sulfite reductases in crude preparations from sulfate-reducing bacteria using polyacrylamide gels. Skyring GW, Trudinger PA. Can J Biochem; 1972 Oct 23; 50(10):1145-8. PubMed ID: 5084357 [No Abstract] [Full Text] [Related]
10. Biochemical studies on sulfate-reducing bacteria. XI. Purification and some properties of sulfite reductase, desulfoviridin. Kobayashi K, Takahashi E, Ishimoto M. J Biochem; 1972 Oct 23; 72(4):879-87. PubMed ID: 4644321 [No Abstract] [Full Text] [Related]
11. Biochemical studies on sulfate-ruducing bacteria. 8. Sulfite reductase from Desulfovibrio vulgaris--mechanism of trithionate, thiosulfate, and sulfide formation and enzymatic properties. Kobayashi K, Seki Y, Ishimoto M. J Biochem; 1974 Mar 23; 75(3):519-29. PubMed ID: 4365884 [No Abstract] [Full Text] [Related]
12. A comparison of the electrophoretic properties of the ATP-sulfurylases, APS-reductases, and sulfite reductases from cultures of dissimilatory sulfate-reducing bacteria. Skyring GW, Trudinger PA. Can J Microbiol; 1973 Mar 23; 19(3):375-80. PubMed ID: 4697263 [No Abstract] [Full Text] [Related]
13. Enzymes involved in the metabolism of thiosulfate by Thiobacillus thioparus. I. Survey of enzymes and properties of sulfite: cytochrome c oxidoreductase. Lyric RM, Suzuki I. Can J Biochem; 1970 Mar 23; 48(3):334-43. PubMed ID: 5438321 [No Abstract] [Full Text] [Related]
14. Regulation of the reduction of sulfite and thiosulfate by ferredoxin, flavodoxin and cytochrome cc' 3 in extracts of the sulfate reducer Desulfovibrio gigas. Hatchikian EC, Le Gall J, Bruschi M, Dubourdieu M. Biochim Biophys Acta; 1972 Mar 08; 258(3):701-8. PubMed ID: 5017697 [No Abstract] [Full Text] [Related]
15. Characterization of a dissimilatory-type sulfite reductase, desulfoviridin, from Desulfovibrio africanus Benghazi. Seki Y, Nagai Y, Ishimoto M. J Biochem; 1985 Dec 08; 98(6):1535-43. PubMed ID: 4093441 [Abstract] [Full Text] [Related]
16. Bisulfite reductase of Desulfovibrio vulgaris: explanation for product formation. Drake HL, Akagi JM. J Bacteriol; 1977 Oct 08; 132(1):139-43. PubMed ID: 914772 [Abstract] [Full Text] [Related]
17. Rubredoxin oxidase, a new flavo-hemo-protein, is the site of oxygen reduction to water by the "strict anaerobe" Desulfovibrio gigas. Chen L, Liu MY, LeGall J, Fareleira P, Santos H, Xavier AV. Biochem Biophys Res Commun; 1993 May 28; 193(1):100-5. PubMed ID: 8503894 [Abstract] [Full Text] [Related]
18. Purification and properties of thiosulfate reductase from Desulfovibrio gigas. Hatchikian EC. Arch Microbiol; 1975 Nov 07; 105(3):249-56. PubMed ID: 242299 [Abstract] [Full Text] [Related]
19. Some physical and kinetic properties of adenylyl sulfate reductase from Desulfovibrio vulgaris. Bramlett RN, Peck HD. J Biol Chem; 1975 Apr 25; 250(8):2979-86. PubMed ID: 235533 [Abstract] [Full Text] [Related]
20. Observations on the bisulfite reductase (P582) isolated from Desulfotomaculum nigrificans. Akagi JM, Chan M, Adams V. J Bacteriol; 1974 Oct 25; 120(1):240-4. PubMed ID: 4424068 [Abstract] [Full Text] [Related] Page: [Next] [New Search]