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PMID: 6430733 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

NADPH-dependent H2O2 generation and peroxidase activity in thyroid particular fraction.

Molecular and cellular endocrinology ·Vol. 36 ·No. 1-2 ·1984-06-00 ·Pages 95-105

Virion A, Michot JL, Deme D, Kaniewski J, Pommier J

Abstract

A NADPH-dependent H2O2 generating system associated with a thyroid particular fraction is described. H2O2 is measured by two different methods: iodination of NADPH itself when the system is supplemented with lactoperoxidase and [125I]iodide, and by the scopoletin method. It is shown that: H2O2 generation is inhibited by catalase and is dependent on NADPH or particulate protein concentration; radical scavengers of OH and of singlet oxygen have no effect while superoxide dismutase has only a marginal effect; disruption of the particular fraction by phospholipase A2 or digitonin treatment completely abolished H2O2 generation activity while thyroid peroxidase activity appears, suggesting different sites for the two activities in the membrane vesicles.

MeSH Terms
Animals Digitonin/pharmacology Free Radicals Hydrogen Peroxide/metabolism In Vitro Techniques Iodides/metabolism NADP/pharmacology NADPH-Ferrihemoprotein Reductase/metabolism Peroxidases/metabolism Phospholipases A/pharmacology Phospholipases A2 Subcellular Fractions/metabolism Swine Thyroid Gland/metabolism
Chemicals
Free Radicals Iodides NADP Hydrogen Peroxide Peroxidases NADPH-tetrazolium reductase NADPH-Ferrihemoprotein Reductase Phospholipases A Phospholipases A2 Digitonin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Virion A
Michot J L
Deme D
Kaniewski J
Pommier J
Article Info
Journal
Molecular and cellular endocrinology
Abbr.
Mol Cell Endocrinol
ISSN
0303-7207
Published
1984-06-00
Pages
95-105
Language
English
Region
Ireland
NLM ID
7500844
Subset
IM
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