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DOI: 10.1177/019262339902700408 Influence of Lead Acetate and Selected Metal Salts on Tryptophan Binding to Rat Hepatic NucleiDepartment of Pathology, George Washington University Medical Center, Washington, D.C. 20037
Department of Pathology, George Washington University Medical Center, Washington, D.C. 20037 This study evaluated whether lead acetate or other selected metal salts would influence the binding of L-tryptophan to rat hepatic nuclei. Lead salts and other salts of cadmium, zinc, mercury, and molybdenum, when added alone, had only small effects on 3H-tryptophan binding to hepatic nuclei in vitro. However, each of these salts, when added along with unlabeled L-tryptophan (excess, 10-4 M), caused significantly less inhibition of 3H-tryptophan binding to hepatic nuclei than did unlabeled L-tryptophan alone. Lead acetate (10 -10 to 10-4 M), when added along with unlabeled L-tryptophan, abrogated the inhibition of binding related to unlabeled L-tryptophan alone. Sodium arsenite (but not potassium arsenate) as well as sodium selenite (at 10 -4 M concentrations) inhibited to a moderate degree the in vitro 3H-tryptophan binding to hepatic nuclei, but addition of 10-4 dithiothreitol, a protective agent for sulfhydryl groups, diminished this inhibition. Rats receiving a high dose of lead acetate before being tube-fed L-tryptophan displayed a decrease in hepatic protein synthesis compared with the stimulatory response connected with L-tryptophan alone. Thus, the addition of lead acetate and of other metal salts appears to have an inhibitory effect on L-tryptophan binding to hepatic nuclei. Lead acetate was investigated in in vivo experiments and was found to negate the stimulation of hepatic protein synthesis related to L-tryptophan alone.
Key Words: Tryptophan • metal cations • liver • nuclear binding • rat
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