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Biochemical characterization and purification of the neuronal sodium-dependent noradrenaline transporter.
- Source :
-
Journal of neural transmission. Supplementum [J Neural Transm Suppl] 1990; Vol. 32, pp. 413-9. - Publication Year :
- 1990
-
Abstract
- The protein properties of the neuronal sodium-dependent noradrenaline (NA) transporter of PC12 (rat pheochromocytoma) cells and of bovine adreno-medullary cells were studied by means of binding of 3H-desipramine (3H-DMI). 3H-DMI binding was decreased by proteases, phospholipase A2, by disulfide reducing agents and by the sulfhydryl-group alkylating agent N-ethylmaleimide. The NA transporter was partially purified by anion exchange and affinity chromatography. Tritiated desmethylxylamine (3H-DMX) bound irreversibly and in a DMI-sensitive manner to two PC12 membrane proteins (32kd and 53kd) which may represent components of the NA transporter.
- Subjects :
- Adrenal Gland Neoplasms metabolism
Adrenal Medulla drug effects
Adrenal Medulla metabolism
Affinity Labels
Animals
Carrier Proteins analysis
Carrier Proteins isolation & purification
Cattle
Cell Membrane drug effects
Cell Membrane metabolism
Cells, Cultured
Desipramine
Disulfides pharmacology
Neurons drug effects
Nitrogen Mustard Compounds pharmacology
Norepinephrine Plasma Membrane Transport Proteins
Pheochromocytoma metabolism
Proteins analysis
Proteins metabolism
Rats
Sulfhydryl Reagents
Sympathomimetics pharmacology
Carrier Proteins metabolism
Neurons metabolism
Norepinephrine metabolism
Sodium physiology
Symporters
Subjects
Details
- Language :
- English
- ISSN :
- 0303-6995
- Volume :
- 32
- Database :
- MEDLINE
- Journal :
- Journal of neural transmission. Supplementum
- Publication Type :
- Academic Journal
- Accession number :
- 2089105
- Full Text :
- https://doi.org/10.1007/978-3-7091-9113-2_56