The in situ size of the dopamine transporter is a tetramer as estimated by radiation inactivation

Biochim Biophys Acta. 1994 Feb 23;1190(1):185-7. doi: 10.1016/0005-2736(94)90051-5.


Radiation inactivation analysis of the mazindol-sensitive binding of the dopamine transporter inhibitor, [3H]GBR-12935 to canine striatal membranes yielded a radiation inactivation target size of 278 +/- 16 kDa. This result, in conjunction with other findings in the literature demonstrating that the molecular mass of the dopamine transporter is approximately 70 kDa, suggests that the native form of the dopamine carrier in the neuronal membranes is a tetrameric assembly of identical 70 kDa subunits.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / antagonists & inhibitors
  • Carrier Proteins / chemistry*
  • Corpus Striatum / metabolism
  • Dogs
  • Dopamine Plasma Membrane Transport Proteins
  • Membrane Glycoproteins*
  • Membrane Transport Proteins*
  • Molecular Weight
  • Nerve Tissue Proteins*
  • Piperazines / metabolism
  • Piperazines / pharmacology*
  • Protein Binding


  • Carrier Proteins
  • Dopamine Plasma Membrane Transport Proteins
  • Membrane Glycoproteins
  • Membrane Transport Proteins
  • Nerve Tissue Proteins
  • Piperazines
  • 1-(2 (diphenylmethoxy)ethyl)-4-(3-phenylpropyl)piperazine