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Updated: Aug 21, 2026

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
Published on: May 10, 2014
ATPase assay of purified, reconstituted CFTR protein
Ilana Kogan1, Mohabir Ramjeesingh, Christine E Bear
1Department of Structural Biology and Biochemistry, The Hospital for Sick Children and Department of Physiology, University of Toronto, Ontario, Canada.
Abstract:
The Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) is a phosphorylation and nucleotide regulated chloride channel. CFTR also directly mediates the hydrolysis of ATP and this catalytic activity is loosely coupled to CFTR channel gating. However, mechanistic detail regarding the role of ATP hydrolysis in channel function is lacking. Our further understanding of the molecular basis for normal channel activity requires kinetic analysis of the ATPase activity by the full-length protein. This article describes an effective assay of ATPase activity by purified, reconstituted CFTR protein.

