Abstract
Publisher Summary 3-Mercaptopyruvate sulfurtransferase catalyzes the cleavage of a carbon–sulfur bond and the transfer of the sulfur atom from 3-mercaptopyruvate to any of a variety of thiophiles, including thiols, cyanide, sulfite, and sulfinates. This chapter deals with the purification of the 3-mercaptopyruvate sulfurtransferase from the bovine kidney. Homogeneous samples of this enzyme use both 2-mercaptoethanol and cyanide as sulfur acceptors; work with other acceptors has not been done. The two assays described in this chapter are (1) assay with 3-mercaptopyruvate as the sulfur donor and 2-mercaptoethanol as the sulfur acceptor substrate; and (2) asssay with 3-mercaptopyruvate as the sulfur donor and cyanide as the sulfur acceptor. In assay one, the production of pyruvate is measured after a reaction with 2,4-dinitrophenylhydrazine. Assay two is based on a calorimetric method for the determination of thiocyanate, one of the reaction products. Although less sensitive, the second method is simpler to perform and is used for routine assay during purification.
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