Affinity purification of the photoreceptor cGMP-gated cation channel

Richard Hurwitz, V. Holcombe

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

The cGMP-gated cation channel is a member of a new family of channel proteins that appear to be directly regulated by cyclic nucleotides. A protein with a subunit molecular mass of 78 kDa that exhibits cGMP-gated calcium flux when reconstituted into phospholipid-containing vesicles has been purified using 8-bromo-cGMP-agarose affinity chromatography. This channel activity is sensitive to the inhibitor l-cis-diltiazem. Treatment of the reconstituted channel with trypsin abolishes the l-cis-diltiazem sensitivity. Apparent endogenous proteolysis can also result in smaller molecular weight polypeptides that exhibit cGMP-gated channel activity but are insensitive to l-cis-diltiazem. These results show that the channel can bind cGMP and that it contains a l-cis-diltiazem inhibitory domain that is distinct from the cGMP-binding domain.

Original languageEnglish (US)
Pages (from-to)7975-7977
Number of pages3
JournalJournal of Biological Chemistry
Volume266
Issue number13
StatePublished - 1991

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Affinity purification of the photoreceptor cGMP-gated cation channel'. Together they form a unique fingerprint.

Cite this