Inhibition of thyroid iodide peroxidase in vivo and in vitro by iproniazid

14C labelled iproniazid binds to iodide peroxidase more effectively in low ionic strength buffer than in high ionic strength buffer, suggesting preferential binding to the monomeric form of iodide peroxidase. During column chromatography, under conditions that separate iodide peroxidase into multiple forms, iproniazid is bound selectively to the monomeric form. Thus, this antithyroid agent appears to bind preferentially to the monomeric enzyme form, or possibly to cause dissociation of the polymeric to the monomeric form.

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Binding of iproniazid to the polymeric forms of iodide peroxidase

Nagasaka

DeGroot

Hidaka

1980

Experientia

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The inactivation of lactoperoxidase and the acyl phosphatase activity of oxidized glyceraldehyde-3-phosphate dehydrogenase by phenylhydrazine and phenyldiimide

Allison

Swain

Tracy

et al. 1973

Archives of Biochemistry and Biophysics

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The effect of inhibitors of thyroid monoamine oxidase on the incorporation of iodide into thyroid slice protein

Huang

Schultz

1972

Life Sciences

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Inhibition of thyroid iodide peroxidase in vivo and in vitro by iproniazid

Cited by 7 publications

References 3 publications

Binding of iproniazid to the polymeric forms of iodide peroxidase

Binding of iproniazid to the polymeric forms of iodide peroxidase

The inactivation of lactoperoxidase and the acyl phosphatase activity of oxidized glyceraldehyde-3-phosphate dehydrogenase by phenylhydrazine and phenyldiimide

The effect of inhibitors of thyroid monoamine oxidase on the incorporation of iodide into thyroid slice protein

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