Inactivation of the catecholamine transporter during the preparation of chromaffin granule membrane 'ghosts'

FEBS Lett. 1987 Sep 28;222(1):215-9. doi: 10.1016/0014-5793(87)80222-3.


The activity of the catecholamine transporter of chromaffin granules and the binding to these vesicles of reserpine, a transporter inhibitor, decrease during ghost preparation. In contrast, the number of binding sites of dihydrotetrabenazine, another transporter ligand, is constant. Dihydrotetrabenazine thus binds to an inactive transporter whereas reserpine binds only to active vesicles. Inactivation occurs during lysis of the granules, possibly because of an incomplete resealing. The turnover number of the transporter, determined by dividing the uptake activity by the density of dihydrotetrabenazine binding sites, has a maximal value (140 molecules/min) in intact granules. The reserpine to dihydrotetrabenazine binding ratio (10-25%) is an estimate of the proportion of correctly resealed vesicles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adrenal Medulla / metabolism
  • Adrenal Medulla / ultrastructure*
  • Animals
  • Carrier Proteins / metabolism*
  • Catecholamine Plasma Membrane Transport Proteins
  • Catecholamines / metabolism*
  • Cattle
  • Cell Fractionation
  • Chromaffin Granules / metabolism
  • Chromaffin Granules / ultrastructure*
  • Chromaffin System / ultrastructure*
  • Intracellular Membranes / metabolism
  • Intracellular Membranes / ultrastructure*
  • Kinetics
  • Membrane Transport Proteins*
  • Norepinephrine / metabolism


  • Carrier Proteins
  • Catecholamine Plasma Membrane Transport Proteins
  • Catecholamines
  • Membrane Transport Proteins
  • Norepinephrine