Characterization of nitrobenzylthioinosine binding sites in the mitochondrial fraction of rat testis

Life Sci. 1996;58(9):753-9. doi: 10.1016/0024-3205(95)02353-4.

Abstract

The presence of [3H] NBMPR binding sites in the mitochondrial fraction of rat testis is described. The dissociation constant (KD) from saturation studies was 0.16 +/- 0.04 nM. The association and dissociation rate constants (k1 and k-1) were 3.95 +/- 0.57 x 10(8) M(-1) min(-1) and 0.025 +/- 0.002 min(-1), respectively. The number of binding sites was 2,100 +/- 163 fmols/mg protein. [3H] NBMPR binding was inhibited, in a nanomolar range, by NBMPR (KI= 0.23 +/- 0.02 nM), OH-NBMPR (KI= 2.30 +/- 0.55 nM) and HNBTG (KI= 2.58 +/- 0.33 nM). In the micromolar range, adenosine receptor ligands such as PIA (3.46 +/- 1.36 microM), 2-chloroadenosine (18.81 +/- 3.36 microM) and NECA (8.26 +/- 3.90 microM), and mitochondrial benzodiazepine receptor ligands such as Ro 5-4864 (5.15 +/- 1.82 micrmoM and PK 11195 inhibited the specific binding of [3H] NBMPR. These results suggest the existence of a nucleoside transport system in the mitochondrial fraction of rat testis.

MeSH terms

  • Affinity Labels / metabolism
  • Animals
  • Binding, Competitive
  • Carrier Proteins / metabolism
  • Male
  • Mitochondria / metabolism*
  • Molecular Structure
  • Radioligand Assay
  • Rats
  • Rats, Sprague-Dawley
  • Sensitivity and Specificity
  • Testis / metabolism*
  • Thioinosine / analogs & derivatives*
  • Thioinosine / metabolism
  • Tritium

Substances

  • Affinity Labels
  • Carrier Proteins
  • Tritium
  • Thioinosine
  • 4-nitrobenzylthioinosine