Detail of "95034-01-8"

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N-Bromoacetylaminocyanopindolol: a highly potent beta-adrenergic affinity label blocks irreversibly a nonprotein component tightly associated with the receptor

N-Bromoacetylaminocyanopindolol: a highly potent beta-adrenergic affinity label blocks irreversibly a nonprotein component tightly associated with the receptor. Chorev, Michael; Feigenbaum, Allan; Keenan, Alan K.Chemical with cas number 95034-01-8 also plays role.; Gilon, Chaim; Levitzki, Alexander (Hadassah Med. Sch., Hebrew Univ., Jerusalem 91-010, Israel). Eur. J. Biochem., 146(1), 9-14 (English) 1985. CODEN: EJBCAI. ISSN: 0014-2956. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Section cross-reference(s): 2 A new chem. affinity label for the b-adrenergic receptor, based on the structure of pindolol, was synthesized and iodinated with 125I. The compd., N-bromoacetylaminocyanopindolol (I) [95034-01-8], has an apparent dissocn. const. of 44 pM towards turkey erythrocyte membranes. I blocks irreversibly both the ability of b-adrenergic receptors to bind 125I-labeled cyanopindolol and the ability of b-receptors to activate adenylate cyclase in the presence of b-agonists. Furthermore, the irreversible binding of I to half of the b-receptor sites abolishes the ligand binding activity of all the sites. These findings suggest that the b-receptor is oligomeric in its native state. Although 125I-labeled I blocks irreversibly and specifically the b-adrenergic receptor, it does so by labeling a nonprotein component, probably a water-sol. lipid. The labeling is stereospecific since it is prevented by l-propranolol and not by d-propranolol. This lipid may be tightly assocd. with the receptor in close proximity to the binding site. This water-sol. lipid fraction may prove crucial for the optimal interaction between the b-adrenergic receptor and the components of adenylate cyclase. .

N-Bromoacetylaminocyanopindolol: a highly potent beta-adrenergic affinity label blocks irreversibly a nonprotein component tightly associated with the receptor

N-Bromoacetylaminocyanopindolol: a highly potent beta-adrenergic affinity label blocks irreversibly a nonprotein component tightly associated with the receptor. Chorev, Michael; Feigenbaum, Allan; Keenan, Alan K.Chemical with cas number 95034-01-8 also plays role.; Gilon, Chaim; Levitzki, Alexander (Hadassah Med. Sch., Hebrew Univ., Jerusalem 91-010, Israel). Eur. J. Biochem., 146(1), 9-14 (English) 1985. CODEN: EJBCAI. ISSN: 0014-2956. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Section cross-reference(s): 2 A new chem. affinity label for the b-adrenergic receptor, based on the structure of pindolol, was synthesized and iodinated with 125I. The compd., N-bromoacetylaminocyanopindolol (I) [95034-01-8], has an apparent dissocn. const. of 44 pM towards turkey erythrocyte membranes. I blocks irreversibly both the ability of b-adrenergic receptors to bind 125I-labeled cyanopindolol and the ability of b-receptors to activate adenylate cyclase in the presence of b-agonists. Furthermore, the irreversible binding of I to half of the b-receptor sites abolishes the ligand binding activity of all the sites. These findings suggest that the b-receptor is oligomeric in its native state. Although 125I-labeled I blocks irreversibly and specifically the b-adrenergic receptor, it does so by labeling a nonprotein component, probably a water-sol. lipid. The labeling is stereospecific since it is prevented by l-propranolol and not by d-propranolol. This lipid may be tightly assocd. with the receptor in close proximity to the binding site. This water-sol. lipid fraction may prove crucial for the optimal interaction between the b-adrenergic receptor and the components of adenylate cyclase. .