Transducin activation in electropermeabilized frog rod outer segments is highly amplified, and a portion equivalent to phosphodiesterase remains membrane-bound.-Reference-Cited by-同舟云学术

Transducin activation in electropermeabilized frog rod outer segments is highly amplified, and a portion equivalent to phosphodiesterase remains membrane-bound.

Published:1990-09 Issue:25 Volume:265 Page:15323-15332
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Gray-Keller M.P.,Biernbaum M.S.,Bownds M.D.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference68 articles.

1. Regulation of membrane-associated and cytosolic phospholipase C activities in human platelets by guanosine triphosphate.

2. Activation of cGMP phosphodiesterase in retinal rods: mechanism of interaction with the GTP-binding protein (transducin)

3. The G-protein of retinal rod outer segments (transducin). Mechanism of interaction with rhodopsin and nucleotides.

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