Identification of Thioredoxin Targeted Proteins Using Thioredoxin Single Cysteine Mutant-immobilized Resin
-
Last Update: 2021-01-16
-
Source: Internet
-
Author: User
Search more information of high quality chemicals, good prices and reliable suppliers, visit
www.echemi.com
Thioredoxins (Trx) are a ubiquitous family of proteins that modulate the enzymatic activity of their substrate proteins by redox regulation. This is achieved by reduction of a disulfide bond within their target proteins. A conserved pair of cysteine residues in Trx is required for catalysis of the dithiol–disulfide exchange with their target proteins. A single-cysteine mutant capable of forming a stable mixed disulfide bond with target proteins was immobilized on resin and used to capture potential target proteins. By using this method, a number of previously unidentified Trx-target protein candidates were captured from various organisms and organelles. Following the development of this technique, more than one hundred proteins have been reported as potential Trx targets, allowing significant progress to be made in our knowledge and understanding of Trx-target proteins.
This article is an English version of an article which is originally in the Chinese language on echemi.com and is provided for information purposes only.
This website makes no representation or warranty of any kind, either expressed or implied, as to the accuracy, completeness ownership or reliability of
the article or any translations thereof. If you have any concerns or complaints relating to the article, please send an email, providing a detailed
description of the concern or complaint, to
service@echemi.com. A staff member will contact you within 5 working days. Once verified, infringing content
will be removed immediately.
