Characterization of the [3H]-desipramine binding site of the bovine adrenomedullary plasma membrane.
Naunyn Schmiedebergs Arch Pharmacol
; 346(2): 203-7, 1992 Aug.
Article
em En
| MEDLINE
| ID: mdl-1333059
ABSTRACT
The specific (i.e. nisoxetine-sensitive) binding of [3H]desipramine was studied in membranes prepared from bovine adrenal medullae. (1) [3H]desipramine bound reversibly and with high affinity (KD = 2.8 nmol/l) to a single class of non-interacting binding sites (Hill coefficient = 0.96); the maximal number of binding sites (Bmax) was 2.1 pmol/mg protein. (2) Binding of [3H]desipramine was dependent on [Na+] and [Cl-]. Increasing the concentrations of these ions increased binding. (3) Substrates and inhibitors of the neuronal noradrenaline transport system (uptake1) inhibited binding of [3H]desipramine with a rank order of potency typical for an interaction with the uptake1 carrier. The characteristics of [3H]desipramine binding remained essentially unchanged after solubilization of adrenomedullary membranes with the non-ionic detergent digitonin. The results indicate that the plasma membrane of bovine adreno-medullary cells is endowed with the neuronal uptake1 transporter.
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Base de dados:
MEDLINE
Assunto principal:
Receptores de Droga
/
Receptores de Neurotransmissores
/
Medula Suprarrenal
/
Simportadores
/
Desipramina
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
Idioma:
En
Ano de publicação:
1992
Tipo de documento:
Article