Measurement of Redox States of the β3 Integrin Disulfide Bonds by Mass Spectrometry

Measurement of Redox States of the β3 Integrin Disulfide Bonds by Mass Spectrometry.

Full text not available from this repository.
Item Type: Article
Status: Published
Official URL:
Journal or Publication Title: BIO-PROTOCOL
Volume: 9
Number: 3
Date: 2019
Divisions: ACRF Centenary Cancer Research Centre
Depositing User: General Admin
Identification Number: 10.21769/BioProtoc.3156
ISSN: 2331-8325
Date Deposited: 17 Dec 2020 02:50

Functional disulfide bonds mediate a change in protein function in which they reside when cleaved or formed. To elucidate how a functional disulfide bond controls protein activity, it is critical that the redox state of the bond in the population of protein molecules is known. Measurement of changes in disulfide bond redox state relies on thiol probes and immunoblotting. Such technique only offers a qualitative indication of a change in redox state but not the identity of cysteines involved. A differential cysteine alkylation and mass spectrometry technique is described here that affords precise quantification of protein disulfide bond redox state. The utility of the technique is demonstrated by quantifying the redox state of 24 of the 28 disulfide bonds in human β3 integrin from purified platelets.

Chiu, Joyce
Last Modified: 17 Dec 2020 02:50

Actions (login required)

View Item View Item