Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2000 Dec 1;116(6):769–780. doi: 10.1085/jgp.116.6.769

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

The Rolf G204W mutant had a slightly greater DAG sensitivity than that of the Brod channel, and its inhibition was similarly voltage-independent (compare with Fig. 4 in companion article, Crary et al. 2000, in this issue). (A) The DAG dose–response curve was measured in the presence of 2 mM cGMP: data were averaged from three patches and fit with the Hill equation. The maximum inhibition for the Rolf G204W mutant was 100% with an IC₅₀ = 0.26 μM and n = 3.2. The Hill fits for the Brod and Rolf channels (from Fig. 4) are shown for comparison as dashed curves. (B) Steady state current–voltage relations obtained from data acquired on a single patch containing the Rolf G204W mutant. Open circles represent cGMP-activated currents at saturating concentrations in the absence of DAG. Filled circles represent currents at saturating cGMP in the presence of 0.8 μM DAG. For comparison, the triangles show the currents at lower (5 μM) cGMP concentration, without DAG.