D-Aspartate Oxidase in the Thyroid Gland

Publisher Website
Google Scholar
Abstract
D-Aspartate oxidase was isolated from the pig thyroid gland and purified over 600 times. The enzyme was obtained in an inactive form of apoenzyme and was activated by FAD. It was specific towards the D-form of aspartic acid, had no effect on the L-form, and was also inactive towards other monocarboxylic D-amino acids. The enzyme was only slightly active towards D-glutamate. The Michaelis constant based on the Lineaweaver-Burk plot was 5 mmol/1. The optimum pH was 8.7. D-Aspartate oxidase was inhibited by KCN in concentrations varying from 0.05 to 1 mmol/1. The biological role of this enzyme in the thyroid gland is discussed.

This publication has 0 references indexed in Scilit: