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The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin
Year:
1985
Source of publication :
FEBS Letters
Authors :
Pines, Mark
;
.
Volume :
182
Co-Authors:
Pines, M., Section on Molecular Pathophysiology, Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Gierschik, P., Section on Molecular Pathophysiology, Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Spiegel, A., Section on Molecular Pathophysiology, Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Facilitators :
From page:
355
To page:
359
(
Total pages:
5
)
Abstract:
The 35-kDa β-subunit of transducin purified from rod outer segment membranes is cleaved into 2 major fragments by trypsin, and 7 major fragments by chymotrypsin. Identical fragments are visualized by immunoblotting with transducin-β specific antisera after proteolysis of rod outer segment membranes, purified brain guanine nucleotide binding proteins, and brain membranes. The results indicate that the β-subunits of transducin and of brain guanine nucleotide binding proteins are not only similar structurally, but are also similarly oriented in membranes with respect to accessibility to proteolytic enzymes. © 1985.
Note:
Related Files :
Animal
Electrophoresis, Polyacrylamide Gel
Peptide Fragments
retina
Transmembrane signalling
visual system
Show More
Related Content
More details
DOI :
10.1016/0014-5793(85)80332-X
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
30508
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:55
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Scientific Publication
The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin
182
Pines, M., Section on Molecular Pathophysiology, Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Gierschik, P., Section on Molecular Pathophysiology, Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Spiegel, A., Section on Molecular Pathophysiology, Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin
The 35-kDa β-subunit of transducin purified from rod outer segment membranes is cleaved into 2 major fragments by trypsin, and 7 major fragments by chymotrypsin. Identical fragments are visualized by immunoblotting with transducin-β specific antisera after proteolysis of rod outer segment membranes, purified brain guanine nucleotide binding proteins, and brain membranes. The results indicate that the β-subunits of transducin and of brain guanine nucleotide binding proteins are not only similar structurally, but are also similarly oriented in membranes with respect to accessibility to proteolytic enzymes. © 1985.
Scientific Publication
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