In Vitro Enzymatic Studies Reveal pH and Temperature Sensitive Properties of the CLIC Proteins.

ABSTRACT: Chloride intracellular ion channel (CLIC) proteins exist as both soluble and integral membrane proteins, with CLIC1 capable of shifting between two distinct structural conformations. New evidence has emerged indicating that members of the CLIC family act as moonlighting proteins, referring to the ability of a single protein to carry out multiple functions. In addition to their ion channel activity, CLIC family members possess oxidoreductase enzymatic activity and share significant structural and sequence homology, along with varying overlaps in their tissue distribution and cellular localization. In this study, the 2-hydroxyethyl disulfide (HEDS) assay system was used to characterize kinetic properties, as well as the temperature and pH profiles of three CLIC protein family members (CLIC1,

SUBMITTER: Alghalayini A 

PROVIDER: S-EPMC10526857 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature