Abstract
The active enzyme catalizing the conversion of L-triiodothyronine to triiodothyroacetic acid has been prepared by repeated freezing and thawing of rat kidney mitochondria, centrifuging, and dialyzing the resulting supernatant. This preparation loses about 50% of its activity by heating at 56 C for 5 minutes. P-chloromercuribenzoate (1.3 × 10−4M) and anoxia are potent inhibitors of the converting enzyme. Cofactors such as FMN, FAD, DPN, α-ketoglutarate, pyruvate, ATP, pyridoxal phosphate, and the combination of α-ketoglutarate or pyruvate with pyridoxal phosphate have no significant effect on the activity of the converting enzyme. It has been found that the converting enzyme is about th as active as the crude untreated L-amino acid oxidase of cobra venom. Michaelis constant (Km) and Vmax of the converting enzyme, measured under specified conditions, are 3.25 × 10−5M and 85 mμ moles/mg N/hour, respectively.
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