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Immobilized rhodanese: some aspects of anion inhibition kinetics and modulation by cations.
Nok, A J; Nasir, S M; Sa Adatu, Y.
J Biochem Toxicol ; 8(2): 57-62, 1993 Jun.
Article in English | MEDLINE | ID: mdl-8355260

ABSTRACT

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.


Subject(s)
Anions/pharmacology , Cations/pharmacology , Enzymes, Immobilized/antagonists & inhibitors , Enzymes, Immobilized/drug effects , Thiosulfate Sulfurtransferase/antagonists & inhibitors , Thiosulfate Sulfurtransferase/drug effects , Acrylic Resins , Animals , Calcium/pharmacology , Enzymes, Immobilized/metabolism , Hydrogen-Ion Concentration , Kinetics , Male , Metals/pharmacology , Rats , Rats, Wistar , Thiosulfate Sulfurtransferase/metabolism
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