Published 1983 | Version v1
Book

Peroxidatic degradation of thyroxine in the microsome fraction of mouse thyroids

  • 1. University of Tokyo (Japan)
  • 2. University of Nagasaki (Japan)

Description

125I-labeled thyroxine (T4) was deiodinated in vitro in the microsome fraction of mouse thyroids when glucose-glucose oxidase was added as a hydrogen peroxide (H2O2) generating system. This degradation of T4 was dependentt of time, temperature, and pH and on the protein concentrations of microsome fraction in dose-related manner. The reaction was inhibited by 10-3M methylmercaptoimidazole (MMI), 10-3M propylthiouracil (PTU), and 600 U/ml catalase. These results suggest that thyroidal peroxidase may catalyse not only iodination of tyrosine but also deiodination of thyroid hormones physiologically

Part of:
Nuclear medicine and biology advances

Additional details

Publishing Information

Publisher
Pergamon Press.
Imprint Place
Paris (France)
ISBN
0-08-026405-0
Imprint Title
Nuclear medicine and biology advances
Imprint Pagination
542 p.
Journal Page Range
v. 4 p. 3470-3473.

Conference

Title
3. World congress of nuclear medicine and biology.
Dates
29 Aug - 2 Sep 1982.
Place
Paris (France).

Optional Information