Mechanism-based inhibition of lactoperoxidase by thiocarbamide goitrogens.

Clicks: 138
ID: 93984
1986
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Star

Ranked #55 of 73 articles by views in Biochemistry

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
The irreversible inactivation of bovine lactoperoxidase by thiocarbamide goitrogens was measured, and the kinetics were consistent with a mechanism-based (suicide) mode. Sulfide ion inactivated, 2-mercaptobenzimidazole-inactivated, and 1-methyl-2-mercaptoimidazole-inactivated lactoperoxidases have different visible spectra, suggesting different products were formed. The results support a mechanism in which reactive intermediates are formed by S-oxygenation reactions catalyzed by lactoperoxidase compound II. It is proposed that the reaction of electron-deficient intermediates with the heme prosthetic group is responsible for the observed spectral changes and inactivation by thiocarbamides.
Reference Key
doerge1986mechanismbasedbiochemistry Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Doerge, D R;
Journal Biochemistry
Year 1986
DOI
DOI not found
URL URL not found
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.