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Referencias:

• Anosike, Jack, Kidney Rhodanese from the guinea pig (Lepus caniculus) and albino rat (Mus musculus) (1982) Enzyme, 27, pp. 33-39
• Anosike, Ugochukwu, Characterization of Rhodanese from cassava leaves and tubers (1981) J. exptl Botany, 32, pp. 1021-1027
• Bergsma, Hol, Jansonius, Kalk, Ploegman, Smit, The double domain structure of Rhodanese (1975) J. mol. Biol., 98, pp. 637-643
• Bowen, Butler, Happold, Some properties of the Rhodanese system of Thiobacillus denitrificans (1965) Biochem. J., 97, pp. 651-657
• Blumenthal, Henrikson, Structural studies of bovine liver Rhodanese (1971) J. biol. Chem., 246, pp. 2430-2437
• Burton, Akagi, Observations on the Rhodanese activity of Desulfotomaculum nigrificans (1971) J. Bacteriol., 107, pp. 375-376
• Canella, Pensa, Pecci, Determination of Rhodanese activity using a pH-STAT apparatus (1975) Analytical Biochemistry, 68, pp. 458-464
• Canella, Costa, Pensa, Ricci, Pecci, Cavallini, Multiple forms of bovine liver Rhodanese (1981) European Journal of Biochemistry, 119, pp. 491-495
• Chew, Boey, Rhodanese of tapioca leaf (1972) Phytochemistry, 11, pp. 167-169
• Cohen-Bazire, Sistrom, Stanier, Kinetic studies of pigment synthesis by non-sulfur purple bacteria (1957) J. cell. comp. Physiol., 49, pp. 25-68
• de Duve, Pressman, Gianetto, Wattiaux, Appelmans, Tissue fractionation studies 6. Intracellular distribution patterns of enzymes in rat-liver tissue (1955) Biochem. J., 60, pp. 604-617
• Jaravak, Westley, Human liver Rhodanese Nonlinear kinetic behaviour in a double displacement mechanism (1974) Biochemistry, 13, pp. 3233-3236
• Le John, Van Caeseele, Lees, Catabolite repression in the facultative chemoautotrophic Thiobacillus novellus (1967) J. Bacteriol., 94, pp. 1484-1491
• Lowry, Rosebrough, Farr, Randall, Protein measurement with the folin phenol regents (1951) J. biol. Chem., 193, pp. 265-275
• Oi, Inhibition of rat liver Rhodanese by ditricarboxilic and α-Keto acids (1975) J. Biochem., 78, pp. 825-834
• Ploegman, Drent, Kalk, Hol, Structure of bovine liver Rhodanese I. The structure determination at 2.5 Å resolution and a comparison of the conformation and sequence of its two domains (1978) J. mol. Biol., 123, pp. 557-594
• Rosenthal, The distribution of Rhodanese (1948) Fedn Proc., 7, pp. 181-182
• Smith, Lascelles, Thiosulphate metabolism and Rhodanese in Chromatium sp. strain D (1966) J. Genet. Microbiol., 42, pp. 357-370
• Sörbo, On the properties of Rhodanese Partial purification inhibitors and intracellular distribution (1951) Acta Chemica Scandinavica, 5, pp. 724-734
• Sörbo, Crystalline Rhodanese I Purification and physicochemical examination (1953) Acta Chemica Scandinavica, 7, pp. 1129-1136
• Tabita, Silver, Lundgren, The Rhodanese enzyme of Ferro-bacillus ferroxidans (1969) Can. J. Biochem., 47, pp. 1141-1145
• Tomati, Federici, Cannella, Rhodanese activity in chloroplasts (1974) Physiol. Chem. Phys., 4, pp. 193-196
• Vanderbergh, Bawdon, Berk, Rapid test for determining the intracellular Rhodanese activity of various Bacteria (1979) International Journal of Systematic Bacteriology, 29, pp. 339-344
• Vanderbergh, Berk, Purification and characterization of Rhodanese from Acinetobacter calcoaceticus (1980) Can. J. Microbiol., 26, pp. 281-286
• van Rensburg, Schabort, Rhodanese from Cercopithecus aethiops (vervet monkey) liver. I. Purification and some physical characteristics (1984) Int. J. Biochem., 16, pp. 539-546
• van Rensburg, Schabort, Rhodanese from Cercopithecus aethiops (vervet monkey) liver II. Aspects of enzyme kinetic and mechanism of action (1984) Int. J. Biochem., 16, pp. 547-551
• Vazquez, Buzaleh, Wider, Batlle, Reduced thiosulphate affinity for erythrocyte Rhodanese: an explanation for increased δ-aminolevulinic synthetase activity in some porphyrias? (1986) IRCS Med. Sci., 14, pp. 999-1000
• Villarejo, Westley, Sulfur metabolism of Bacillus subtilis (1966) Biochim. biophys. Acta, 117, pp. 209-216
• Volini, de Toma, Westley, Dimeric structure and zinc content of bovine liver Rhodanese (1967) J. biol. Chem., 242, pp. 5220-5225
• Volini, Craven, Ogata, The different molecular weight forms of bovine liver Rhodanese (1978) J. biol. Chem., 253, pp. 7591-7594
• Watanabe, Nakano, Kitaoka, Subcellular location and some properties of Rhodanese in Euglena gracilis (1985) Agricultural and Biological Chemistry, 49, pp. 2203-2204
• Westley, A comparison of some biochemical properties of the beef liver and beef kidney Rhodanese (1959) J. biol. Chem., 234, pp. 1857-1860
• Westley, (1973) Rhodanese in Advances in Enzymology, 39, pp. 327-368. , A. Meister, Interscience, New York
• Westley, Heyse, Mechanisms of sulfur transfer catalysis. Sulphydryl-catalyzed transfer of thiosulfonate sulfur (1971) J. biol. Chem., 246, pp. 1468-1474
• Wider de Xifra, Sandy, Davies, Neuberger, Control of Δ-aminolaevulinate synthetase activity in Rhodopseudomonas spheroides (1976) Phil. Trans. R. Soc. Lond. B, 273, pp. 79-98

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