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

. 2004 Jun;123(6):729–741. doi: 10.1085/jgp.200308994

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

Copyright © 2004, 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

Figure 8. — Calculated flash responses. (A) Assumed time courses of rhodopsin's catalytic activity. In the control rod (top), activity shut off exponentially after a delay of 100 ms (Chen et al., 1995b, 1999). The time constant of 205 ms was found from the mean slope of the relation between T_sat and the natural logarithm of the flash strength (compare Pepperberg et al., 1992). In the rec−/− rod (bottom), rhodopsin activity suddenly fell ninefold after 100 ms and then decayed exponentially with a time constant of 205 ms. (B) Photocurrents generated by the flash response model () for control (thick traces) and rec−/− (thin traces) rods. Rhodopsin's catalytic activity was increased ten-fold for successive pairs of responses. (C) Responses from the model in the absence of Ca²⁺ feedback onto guanylate cyclase for rods with (thick traces) and without (thin traces) recoverin. The catalytic activity levels of rhodopsin are the same as those in B.