YEAST RNA-POLYMERASE .1. A EUKARYOTIC ZINC METALLOENZYME
dc.contributor.author | AULD, DS | |
dc.contributor.author | ATSUYA, I | |
dc.contributor.author | CAMPINO, C | |
dc.contributor.author | VALENZUELA, P | |
dc.date.accessioned | 2025-01-23T19:45:00Z | |
dc.date.available | 2025-01-23T19:45:00Z | |
dc.date.issued | 1976 | |
dc.description.abstract | Microwave excitation spectrometry and metal binding inhibition studies showed that Zn is a catalytically essential component of the highly purified RNA polymerase I from yeast, the 1st eukaryotic RNA polymerase I available in quantities sufficient for such studies. It contained 2.4 g-atom of Zn based on a MW of 6.5 .times. 105. Cu, Fe, Mn and Mg were absent, i.e., below the limits of detection, 10-3-10-14 g-atoms. A number of derivatives of 1,10-phenanthroline reversibly inhibited the polymerase catalyzed reaction, apparently by forming a ternary polymerase.cntdot.Zn.cntdot.OP complex while the nonchelating isomer, 1,7-phenanthroline, was ineffective. | |
dc.fuente.origen | WOS | |
dc.identifier.eissn | 1090-2104 | |
dc.identifier.issn | 0006-291X | |
dc.identifier.uri | https://repositorio.uc.cl/handle/11534/100179 | |
dc.identifier.wosid | WOS:A1976BN09600038 | |
dc.issue.numero | 2 | |
dc.language.iso | en | |
dc.pagina.final | 554 | |
dc.pagina.inicio | 548 | |
dc.revista | Biochemical and biophysical research communications | |
dc.rights | acceso restringido | |
dc.subject.ods | 03 Good Health and Well-being | |
dc.subject.odspa | 03 Salud y bienestar | |
dc.title | YEAST RNA-POLYMERASE .1. A EUKARYOTIC ZINC METALLOENZYME | |
dc.type | artículo | |
dc.volumen | 69 | |
sipa.index | WOS | |
sipa.trazabilidad | WOS;2025-01-12 |