{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T16:41:51Z","timestamp":1777912911296,"version":"3.51.4"},"reference-count":45,"publisher":"SAGE Publications","issue":"4","license":[{"start":{"date-parts":[[1999,7,1]],"date-time":"1999-07-01T00:00:00Z","timestamp":930787200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxicol Pathol"],"published-print":{"date-parts":[[1999,7]]},"abstract":"<jats:p>\n                    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\n                    <jats:sup>3<\/jats:sup>\n                    H-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\n                    <jats:sup>3<\/jats:sup>\n                    H-tryptophan binding to hepatic nuclei than did unlabeled L-tryptophan alone. Lead acetate (10\n                    <jats:sup>-10<\/jats:sup>\n                    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\n                    <jats:sup>-4<\/jats:sup>\n                    M concentrations) inhibited to a moderate degree the in vitro\n                    <jats:sup>3<\/jats:sup>\n                    H-tryptophan binding to hepatic nuclei, but addition of 10\n                    <jats:sup>-4<\/jats:sup>\n                    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.\n                  <\/jats:p>","DOI":"10.1177\/019262339902700408","type":"journal-article","created":{"date-parts":[[2008,2,8]],"date-time":"2008-02-08T19:38:42Z","timestamp":1202499522000},"page":"441-447","source":"Crossref","is-referenced-by-count":2,"title":["Influence of Lead Acetate and Selected Metal Salts on Tryptophan Binding to Rat Hepatic Nuclei"],"prefix":"10.1177","volume":"27","author":[{"given":"Herschel","family":"Sidransky","sequence":"first","affiliation":[{"name":"Department of Pathology, George Washington University Medical Center, Washington, D.C. 20037"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ethel","family":"Verney","sequence":"additional","affiliation":[{"name":"Department of Pathology, George Washington University Medical Center, Washington, D.C. 20037"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[1999,7,1]]},"reference":[{"key":"atypb1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1920085"},{"key":"atypb2","doi-asserted-by":"publisher","DOI":"10.1126\/science.154.3757.1662"},{"key":"atypb3","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2787(68)90362-6"},{"key":"atypb4","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)49919-5"},{"key":"atypb5","doi-asserted-by":"publisher","DOI":"10.1042\/bst0021251"},{"key":"atypb6","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM199809173391214"},{"key":"atypb7","first-page":"669","volume":"26","author":"Kurl RN","year":"1987","journal-title":"Nutr. 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