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פותח על ידי קלירמאש פתרונות בע"מ -
Chemical characterization of ligand binding site fragments from turkey β-adrenergic receptor
Year:
1989
Source of publication :
FEBS Letters
Authors :
אשדת, יובל
;
.
Volume :
246
Co-Authors:
Eshdat, Y., Laboratoire de Biologie Moléculaire des Récepteurs, Centre National de la Recherche Scientifique, Université de Paris VII, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France
Chapot, M.-P., Laboratoire de Biologie Moléculaire des Récepteurs, Centre National de la Recherche Scientifique, Université de Paris VII, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France
Strosberg, A.D., Laboratoire de Biologie Moléculaire des Récepteurs, Centre National de la Recherche Scientifique, Université de Paris VII, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France
Facilitators :
From page:
166
To page:
170
(
Total pages:
5
)
Abstract:
Affinity-labeled β-adrenergic receptor from turkey erythrocyte membranes was specifically cleaved near cysteine residues after S-cyanylation. Analysis of the labeled polypeptide fragments suggests that iodocyanopindolol diazirine reacted with an amino acid residue which is located in the non-glycosylated region containing the sixth and seventh transmembrane domains of the receptor. However, the possibility cannot be excluded that a second residue, located between the third and fifth transmembrane domains, was also labeled. Since treatment with either hydroxylamine or triethylamine resulted in removal of the affinity label from the protein, the present study suggests that aspartic or glutamic acid residues are present in the adrenergic-binding site which is located in the above-mentioned domains. The procedure for specific chemical cleavage of the affinity-labeled adrenergic receptor should also be useful for future structural and comparative studies of other adrenergic receptors. © 1989.
Note:
Related Files :
Animal
erythrocyte membrane
Ethylamines
Glycoside Hydrolases
Hydroxylamines
Peptide Fragments
Receptor
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/0014-5793(89)80276-5
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
32217
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:08
Scientific Publication
Chemical characterization of ligand binding site fragments from turkey β-adrenergic receptor
246
Eshdat, Y., Laboratoire de Biologie Moléculaire des Récepteurs, Centre National de la Recherche Scientifique, Université de Paris VII, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France
Chapot, M.-P., Laboratoire de Biologie Moléculaire des Récepteurs, Centre National de la Recherche Scientifique, Université de Paris VII, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France
Strosberg, A.D., Laboratoire de Biologie Moléculaire des Récepteurs, Centre National de la Recherche Scientifique, Université de Paris VII, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France
Chemical characterization of ligand binding site fragments from turkey β-adrenergic receptor
Affinity-labeled β-adrenergic receptor from turkey erythrocyte membranes was specifically cleaved near cysteine residues after S-cyanylation. Analysis of the labeled polypeptide fragments suggests that iodocyanopindolol diazirine reacted with an amino acid residue which is located in the non-glycosylated region containing the sixth and seventh transmembrane domains of the receptor. However, the possibility cannot be excluded that a second residue, located between the third and fifth transmembrane domains, was also labeled. Since treatment with either hydroxylamine or triethylamine resulted in removal of the affinity label from the protein, the present study suggests that aspartic or glutamic acid residues are present in the adrenergic-binding site which is located in the above-mentioned domains. The procedure for specific chemical cleavage of the affinity-labeled adrenergic receptor should also be useful for future structural and comparative studies of other adrenergic receptors. © 1989.
Scientific Publication
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