{"title":"几种农药对碳酸酐酶同工酶影响的研究","authors":"Aybike Baltacı, Kubra Cıkrıkcı, Nahit Gençer","doi":"10.1002/jmr.3048","DOIUrl":null,"url":null,"abstract":"<p>The aim of this study was to investigate the inhibitory effects of some pesticides known to have harmful effects on human health on carbonic anhydrase isoenzymes. Therefore, carbonic anhydrase isoenzymes (hCA I and II) were purified from human erythrocytes. The isoenzymes were purified from human erythrocytes by using an affinity column that has the chemical structure of Sepharose-4B-4-(6-amino-hexyloxy)-benzenesulfonamide. The purity of the isoenzymes was checked by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDSPAGE). It was determined that the pesticides used in this study inhibit hCA I and hCA II isoenzymes at different levels in vitro. It was determined that the strongest inhibitor for the hCA I enzyme was Carbofuran (IC<sub>50</sub>:6.52 μM; <i>K</i><sub><i>i</i></sub>: 3.58 μM) and the weakest one was 1-Naphtol (IC<sub>50</sub>:16.55 μM; <i>K</i><sub><i>i</i></sub>: 14.4 μM) among these pesticides. It was also found that the strongest inhibitor for the hCA II enzyme was coumatetralil (IC<sub>50</sub>:5.06 μM; <i>K</i><sub><i>i</i></sub>: 1.62 μM) and the weakest one was Dimethachlor (IC<sub>50</sub> 14.6 μM; <i>K</i><sub><i>i</i></sub>: 8.44 μM).</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"36 9","pages":""},"PeriodicalIF":2.3000,"publicationDate":"2023-08-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Investigation of the effects of some pesticides on carbonic anhydrase isoenzymes\",\"authors\":\"Aybike Baltacı, Kubra Cıkrıkcı, Nahit Gençer\",\"doi\":\"10.1002/jmr.3048\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>The aim of this study was to investigate the inhibitory effects of some pesticides known to have harmful effects on human health on carbonic anhydrase isoenzymes. Therefore, carbonic anhydrase isoenzymes (hCA I and II) were purified from human erythrocytes. The isoenzymes were purified from human erythrocytes by using an affinity column that has the chemical structure of Sepharose-4B-4-(6-amino-hexyloxy)-benzenesulfonamide. The purity of the isoenzymes was checked by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDSPAGE). It was determined that the pesticides used in this study inhibit hCA I and hCA II isoenzymes at different levels in vitro. It was determined that the strongest inhibitor for the hCA I enzyme was Carbofuran (IC<sub>50</sub>:6.52 μM; <i>K</i><sub><i>i</i></sub>: 3.58 μM) and the weakest one was 1-Naphtol (IC<sub>50</sub>:16.55 μM; <i>K</i><sub><i>i</i></sub>: 14.4 μM) among these pesticides. It was also found that the strongest inhibitor for the hCA II enzyme was coumatetralil (IC<sub>50</sub>:5.06 μM; <i>K</i><sub><i>i</i></sub>: 1.62 μM) and the weakest one was Dimethachlor (IC<sub>50</sub> 14.6 μM; <i>K</i><sub><i>i</i></sub>: 8.44 μM).</p>\",\"PeriodicalId\":16531,\"journal\":{\"name\":\"Journal of Molecular Recognition\",\"volume\":\"36 9\",\"pages\":\"\"},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2023-08-08\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Molecular Recognition\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/jmr.3048\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Recognition","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/jmr.3048","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Investigation of the effects of some pesticides on carbonic anhydrase isoenzymes
The aim of this study was to investigate the inhibitory effects of some pesticides known to have harmful effects on human health on carbonic anhydrase isoenzymes. Therefore, carbonic anhydrase isoenzymes (hCA I and II) were purified from human erythrocytes. The isoenzymes were purified from human erythrocytes by using an affinity column that has the chemical structure of Sepharose-4B-4-(6-amino-hexyloxy)-benzenesulfonamide. The purity of the isoenzymes was checked by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDSPAGE). It was determined that the pesticides used in this study inhibit hCA I and hCA II isoenzymes at different levels in vitro. It was determined that the strongest inhibitor for the hCA I enzyme was Carbofuran (IC50:6.52 μM; Ki: 3.58 μM) and the weakest one was 1-Naphtol (IC50:16.55 μM; Ki: 14.4 μM) among these pesticides. It was also found that the strongest inhibitor for the hCA II enzyme was coumatetralil (IC50:5.06 μM; Ki: 1.62 μM) and the weakest one was Dimethachlor (IC50 14.6 μM; Ki: 8.44 μM).
期刊介绍：
Journal of Molecular Recognition (JMR) publishes original research papers and reviews describing substantial advances in our understanding of molecular recognition phenomena in life sciences, covering all aspects from biochemistry, molecular biology, medicine, and biophysics. The research may employ experimental, theoretical and/or computational approaches.
The focus of the journal is on recognition phenomena involving biomolecules and their biological / biochemical partners rather than on the recognition of metal ions or inorganic compounds. Molecular recognition involves non-covalent specific interactions between two or more biological molecules, molecular aggregates, cellular modules or organelles, as exemplified by receptor-ligand, antigen-antibody, nucleic acid-protein, sugar-lectin, to mention just a few of the possible interactions. The journal invites manuscripts that aim to achieve a complete description of molecular recognition mechanisms between well-characterized biomolecules in terms of structure, dynamics and biological activity. Such studies may help the future development of new drugs and vaccines, although the experimental testing of new drugs and vaccines falls outside the scope of the journal. Manuscripts that describe the application of standard approaches and techniques to design or model new molecular entities or to describe interactions between biomolecules, but do not provide new insights into molecular recognition processes will not be considered. Similarly, manuscripts involving biomolecules uncharacterized at the sequence level (e.g. calf thymus DNA) will not be considered.
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