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3.
Arch Biochem Biophys ; 361(2): 202-6, 1999 Jan 15.
Article in English | MEDLINE | ID: mdl-9882447

ABSTRACT

Incubation of bovine liver mitochondrial rhodanese in dilute, reducing solutions at temperatures ranging between 30 and 45 degreesC conduced to a rapid loss of enzymatic activity. This inactivation was substantially reduced in the presence of millimolar concentrations of alkali metal ions, divalent cations (including Mg2+, Ca2+, and Ba2+) were ineffective. The extent of protection afforded by monovalent cations was highly dependent on their ionic radii, with K+ and Na+ ions being the most effective protective agents. The protection afforded by a number of anions, including thiosulfate, could be totally ascribed to the presence of the accompanying monovalent cation. The overall results indicate that K+ and Na+, at concentrations and temperatures within the physiological range, substantially contribute to the stabilization of the functional structure of rhodanese.


Subject(s)
Hot Temperature , Metals, Alkali/pharmacology , Mitochondria, Liver/drug effects , Mitochondria, Liver/enzymology , Thiosulfate Sulfurtransferase/metabolism , Animals , Cattle , Enzyme Activation/drug effects , Enzyme Stability/drug effects , Potassium/pharmacology , Salts/pharmacology , Sodium/pharmacology , Thiosulfates/pharmacology
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