The identification and purification of the heterotrimeric GTP-binding protein from squid (Loligo forbesi) photoreceptors
- 1 October 1991
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 279 (1) , 323-326
- https://doi.org/10.1042/bj2790323
Abstract
The principal GTP-binding protein (G-protein) from squid (Loligo forbesi) photoreceptor membranes has been identified by amino acid sequencing. The heterotrimeric protein was purified by detergent solubilization and ion-exchange chromatography. The amino acid sequence of the G-protein alpha-subunit (G-alpha) indicates that this subunit is closely related to the recently characterized Gq subgroup, whereas the G-gamma subunit varies widely in sequence from other homologues.Keywords
This publication has 30 references indexed in Scilit:
- Regulation of Polyphosphoinositide-specific Phospholipase C Activity by Purified G qScience, 1991
- dgq: A drosophila gene encoding a visual system-specific Gα moleculeNeuron, 1990
- G protein multiplicity in eukaryotic signal transduction systemsBiochemistry, 1988
- Octopus rhodopsin Amino acid sequence deduced from cDNAFEBS Letters, 1988
- G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALSAnnual Review of Biochemistry, 1987
- Blockade of Visual Excitation and Adaptation in Limulus Photoreceptor by GDP-β-SScience, 1986
- The Drosophila ninaE gene encodes an opsinCell, 1985
- myo-inositol polyphosphate may be a messenger for visual excitation in Limulus photoreceptorsNature, 1984
- Photoreceptor excitation and adaptation by inositol 1,4,5-trisphosphateNature, 1984
- Light-regulated biochemical events in invertebrate photoreceptors. 1. Light-activated guanosine triphosphatase, guanine nucleotide binding, and cholera toxin-catalyzed labeling of squid photoreceptor membranesBiochemistry, 1984