1. Rhodanese has been extracted from Thiobacillus denitrificans by ultrasonic disintegration of the cells. 2. Studies with Sephadex columns have shown that the enzyme aggregates, forming a tetramer. 3. The molecular weights of the monomer and of an enzymically active sub-unit one-quarter this size have been determined by gel filtration. 4. Higher-molecular-weight forms of rhodanese are broken down by mercaptoethanol to enzymically active fragments of mol.wt. 7000 and 2000 respectively. 5. It is suggested that these fragments are linked in vivo via disulphide bridges to form the monomer, which can then aggregate via further disulphide links. 6. The fragment of mol.wt. 7000 has been obtained in a substantially pure state. 7. Both disulphide and thiol groups are necessary for enzyme activity. 8. Similarities and differences existing between bacterial rhodanese, mammalian rhodanese and β-mercaptopyruvate sulphurtransferase are discussed.
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