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.
Nok
A J
AJ
Department of Biochemistry, Ahmadu Bello University, Zaria, Nigeria.
Nasir
S M
SM
Sa Adatu
Y
Y
D000180:Acrylic Resins; D000818:Animals; D000838:Anions / Q000494:pharmacology*; D002118:Calcium / Q000494:pharmacology; D002412:Cations / Q000494:pharmacology*; D004800:Enzymes, Immobilized / Q000037:antagonists & inhibitors* / Q000187:drug effects* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D008670:Metals / Q000494:pharmacology; D051381:Rats; D017208:Rats, Wistar; D013884:Thiosulfate Sulfurtransferase / Q000037:antagonists & inhibitors* / Q000187:drug effects* / Q000378:metabolism
D000180:Acrylic Resins; D000838:Anions; D002412:Cations; D004800:Enzymes, Immobilized; D008670:Metals; C016680:polyacrylamide gels; D013884:Thiosulfate Sulfurtransferase; D002118:Calcium