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Amino Acids

, Volume 18, Issue 2, pp 103–116 | Cite as

Effect of cycloheximide on tryptophan binding to rat hepatic nuclei

  • H. Sidransky
  • E. Verney

Summary.

This study evaluated whether cycloheximide, an inhibitor of protein synthesis, would affect the binding of L-tryptophan to rat hepatic nuclei or nuclear envelopes. Previous reports have indicated that the binding of L-tryptophan to hepatic nuclear envelope protein was saturable, stereospecific, and of high affinity. Also, the administration of L-tryptophan rapidly stimulated hepatic protein synthesis. In this study, we determined that the addition of cycloheximide in vitro inhibited 3H-tryptophan binding to hepatic nuclei or nuclear envelopes. Heat-treated cycloheximide failed to have this inhibitory binding effect. In vivo treatment of rats with cycloheximide diminished in vitro 3H-tryptophan binding to hepatic nuclei of treated rats compared to controls. Puromycin, another inhibitor of hepatic protein synthesis, when added in vitro did not affect 3H-tryptophan binding to hepatic nuclei but did diminish in vitro binding after in vivo treatment. Thus, cycloheximide added in vitro diminished 3H-tryptophan binding to hepatic nuclei probably by its structural effect on the receptor while cycloheximide administered in vivo may also act in part by inhibiting protein synthesis.

Keywords: Amino acids – L-tryptophan – Hepatic nuclear binding – Cycloheximide – Rats 

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Copyright information

© Springer-Verlag Wien 2000

Authors and Affiliations

  • H. Sidransky
    • 1
  • E. Verney
    • 1
  1. 1.Department of Pathology, George Washington University Medical Center, Washington, District of Columbia, U.S.A.US

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