Regulation of Rod GTP Binding Protein by Guanine Nucleotides

The rod GTP-binding protein in the bovine disk membrane seems to exist as oligomers in the dark. Gα and Gβ do not interact strongly, and Gγ may be required for Gα·GDP to dimerize.

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Bibliographic Details
Published inJournal of biochemistry (Tokyo) Vol. 96; no. 5; pp. 1633 - 1636
Main Authors SHICHI, Hitoshi, SOMERS, Robert L.
Format Journal Article
LanguageEnglish
Published Oxford Oxford University Press 01.01.1984
Subjects
Analytical, structural and metabolic biochemistry
Animals
Binding and carrier proteins
Biological and medical sciences
Cattle
Chemical Phenomena
Chemistry
Chromatography, Gel
Fundamental and applied biological sciences. Psychology
GTP-binding protein
GTP-Binding Proteins - isolation & purification
GTP-Binding Proteins - metabolism
guanine nucleotides
Guanine Nucleotides - pharmacology
Peptide Fragments
Photoreceptor Cells - metabolism
Proteins
retina
rod outer segment membranes
Binding protein
Rhodopsin
Bovine
Molecular structure
Animal
Rod
Guanine nucleotide
Molecular interaction
Retina
Oligomer
Structure function relationship
Photochemistry
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Summary:The rod GTP-binding protein in the bovine disk membrane seems to exist as oligomers in the dark. Gα and Gβ do not interact strongly, and Gγ may be required for Gα·GDP to dimerize.
Bibliography:1This work was presented at U.S.-Japan Visual Pigment Workshop held at Hawaii in January, 1984. Supported by NIH grant EY 03807.
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ArticleID:96.5.1633
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ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a134994