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Nok, A.J. et al.

Immobilized rhodanese: some aspects of anion inhibition kinetics and modulation by cations.

The rat liver rhodanese (thiosulphate: cyanide sulfurtransferase EC 2.6.1.1) has been immobilized on polyacrylamide gels. The immobilized enzyme had a pH optimum of 7.4 and Km values of 3.25 mM and 1.12 mM for S2O3(2-) and KCN, respectively. The enzyme was competitively inhibited by NaNO2 and CH3COONa and noncompetitively by amyl-nitrite. A modulation of activity was observed in the presence of Ca2+, Zn2+, and Cu2+. The results are discussed in line with the detoxicating function of liver rhodanese.[1]

References

Immobilized rhodanese: some aspects of anion inhibition kinetics and modulation by cations. Nok, A.J., Nasir, S.M., Sa Adatu, Y. J. Biochem. Toxicol. (1993) [Pubmed]

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