THE PH-DEPENDENCE OF RAT-LIVER RNA POLYMERASE-I AND POLYMERASE-II

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dc.contributor.authorBULL, P
dc.contributor.authorMARTIAL, J
dc.contributor.authorTELLEZ, R
dc.contributor.authorVENEGAS, A
dc.contributor.authorVALENZUELA, P
dc.date.accessioned2025-01-23T19:44:28Z
dc.date.available2025-01-23T19:44:28Z
dc.date.issued1980
dc.description.abstractThe effect of pH on the stability and activity of rat liver RNA polymerases I (A) and II (B) was studied. Both enzymes are irreversibly inactivated in buffer solutions below pH 5.0. Km values of the 2 enzymes are constant between pH 6.5 and 8.7, but a 2- to 3-fold increase is observed between pH 8.7 and 9.7. The Vmax vs. pH profiles are bell-shaped curves indicating the participation of 2 ionizing groups with apparent pKa values of 6.5 and 9.8 for enzyme I and 6.7 and 9.9 for enzyme II. Both enzymes are inactivated by photooxidation in the presence of Rose Bengal. The above pKa corresponds to the imidazole of a histidine residue and an amino group of a lysine residue.
dc.fuente.origenWOS
dc.identifier.issn0004-0533
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/100050
dc.identifier.wosidWOS:A1980LE27000008
dc.issue.numero2
dc.language.isoen
dc.pagina.final269
dc.pagina.inicio265
dc.revistaArchivos de biologia y medicina experimentales
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleTHE PH-DEPENDENCE OF RAT-LIVER RNA POLYMERASE-I AND POLYMERASE-II
dc.typeartículo
dc.volumen13
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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