Book/Report

FZJ-2018-02584

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Lichtabhängiger Nukleotidaustausch an der Photorezeptormembran und seine Katalyse durch Rhodopsin

Wehner, M. (Corresponding author)FZJ*

1986
Kernforschungsanlage Jülich, Verlag Jülich

Please use a persistent id in citations: http://hdl.handle.net/2128/18277

Report No.: Juel-2044

Abstract: 1) The ability of bleached rhodopsin (Rh*) to mediate light induced binding of $^{3}$H-GTP, or of some GTP-analogues to the $\alpha$-subunit of transducin (T$_{\alpha}$$_{\beta}$$_{\gamma}$) was measured in tracer experiments using filtration methods. Whole rod outer segments (ROS) were compared with areconstituted system consisting of washed membranes with added peripheral proteins (mainly T and PDE). Bleaching 1% of the rhodopsin ieads to a maximumnucleotide binding reaction an T$_{\alpha}$ in both systems. In experiments with whole ROS half-maximum binding of $^{3}$H-GNP to T$_{\alpha}$ occurred at a bleaching rate of 0.0263 % (respectively at 0.0229 % Rh* in a second preparation). The corresponding values for the reconstituted system were observed at bleaching degrees of 0.0234 % (respectively 0.0372 %) Rh*. The resulting amplification factors - that means the number of bound $^{3}$H-GNP catalyzed by one Rh* - were 129 (respectively 122 in a second preparation) molecules $^{3}$H-GNP$_{bound}$/Rh* in whole ROS, and 114 (respectively 70) molecules $^{3}$H-GNP$_{bound}$/Rh* in the reconstituted system. [...]

---

Contributing Institute(s):

1. Publikationen vor 2000 (PRE-2000)

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

---

Database coverage:

---