Michael E. Friedman, Paul Melius, John E. Teggins, Charles A. McAuliffe
{"title":"顺式和反式铂(II)配合物在不同单核苷酸和多核苷酸存在下与脱氢酶的相互作用:三元配合物的证据","authors":"Michael E. Friedman, Paul Melius, John E. Teggins, Charles A. McAuliffe","doi":"10.1016/S0006-3061(00)80167-2","DOIUrl":null,"url":null,"abstract":"<div><p>The inhibition of several dehydrogenase enzymes by <em>cis</em>- and <em>trans</em>- Pt(NH<sub>3</sub>)<sub>2</sub>Cl<sub>2</sub> have been measured in the presence of baker yeast ribonucleic acid (RNA), calf thymus and salmon sperm deoxyribonuclic acid (DNA) and several mononucleotides (AMP and ATP). The binding constants for the interaction of the platinum complexes to the nucleotides have been calculated and a comparison of those values to the previously calculated platinum complex-enzyme binding constants strongly suggest that platinum compounds are more tightly bound to the enzymes. The binding of the platinum complexes to most of the enzymes was decreased in the presence of any nucleotide, yet it was observed that when using rabbit muscle (M<sub>4</sub>) lactate dehydrogenase the mononucleotides reduced the binding to a lesser degree while the polynucleotides actually enhanced the platinum-enzyme interaction. The implications of these interactions are discussed.</p></div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 4","pages":"Pages 341-353"},"PeriodicalIF":0.0000,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80167-2","citationCount":"10","resultStr":"{\"title\":\"Interactions of Cis- and Trans-platinum(II) complexes with dehydrogenase enzymes in the presence of different mono- and polynucleotides: Evidence for a ternary complex\",\"authors\":\"Michael E. Friedman, Paul Melius, John E. Teggins, Charles A. McAuliffe\",\"doi\":\"10.1016/S0006-3061(00)80167-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The inhibition of several dehydrogenase enzymes by <em>cis</em>- and <em>trans</em>- Pt(NH<sub>3</sub>)<sub>2</sub>Cl<sub>2</sub> have been measured in the presence of baker yeast ribonucleic acid (RNA), calf thymus and salmon sperm deoxyribonuclic acid (DNA) and several mononucleotides (AMP and ATP). The binding constants for the interaction of the platinum complexes to the nucleotides have been calculated and a comparison of those values to the previously calculated platinum complex-enzyme binding constants strongly suggest that platinum compounds are more tightly bound to the enzymes. The binding of the platinum complexes to most of the enzymes was decreased in the presence of any nucleotide, yet it was observed that when using rabbit muscle (M<sub>4</sub>) lactate dehydrogenase the mononucleotides reduced the binding to a lesser degree while the polynucleotides actually enhanced the platinum-enzyme interaction. The implications of these interactions are discussed.</p></div>\",\"PeriodicalId\":9177,\"journal\":{\"name\":\"Bioinorganic chemistry\",\"volume\":\"8 4\",\"pages\":\"Pages 341-353\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1978-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80167-2\",\"citationCount\":\"10\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioinorganic chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0006306100801672\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioinorganic chemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0006306100801672","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Interactions of Cis- and Trans-platinum(II) complexes with dehydrogenase enzymes in the presence of different mono- and polynucleotides: Evidence for a ternary complex
The inhibition of several dehydrogenase enzymes by cis- and trans- Pt(NH3)2Cl2 have been measured in the presence of baker yeast ribonucleic acid (RNA), calf thymus and salmon sperm deoxyribonuclic acid (DNA) and several mononucleotides (AMP and ATP). The binding constants for the interaction of the platinum complexes to the nucleotides have been calculated and a comparison of those values to the previously calculated platinum complex-enzyme binding constants strongly suggest that platinum compounds are more tightly bound to the enzymes. The binding of the platinum complexes to most of the enzymes was decreased in the presence of any nucleotide, yet it was observed that when using rabbit muscle (M4) lactate dehydrogenase the mononucleotides reduced the binding to a lesser degree while the polynucleotides actually enhanced the platinum-enzyme interaction. The implications of these interactions are discussed.