The interaction of yeast RNA polymerase I and Cibacron blue F3GA

Paulina Bull, Heather MacDonald, Pablo Valenzuela

Resultado de la investigación: Article

9 Citas (Scopus)

Resumen

The interaction between yeast RNA polymerase I and Cibacron blue F3GA has been studied by difference spectrophotometry and column chromatography. The enzyme is reversibly inhibited by the dye. 50% inhibition is obtained with 7.5 · 10-6 M Cibacron blue. 1 mol Cibacron blue binds per mol enzyme. This interaction, which is inhibited by salt, occurs at a site different from the active site. When RNA polymerase I is chromatographed in Blue dextran-Sepharose columns, two polypeptides, of 48 000 and 36 000 daltons, are dissociated from the enzyme. The resulting enzyme is completely inactive. ATP (5 mM) present in the elution buffer prevents both the dissociation of the polypeptides and the inactivation of the enzyme.

Idioma originalEnglish
Páginas (desde-hasta)368-377
Número de páginas10
PublicaciónBBA Section Nucleic Acids And Protein Synthesis
Volumen653
N.º3
DOI
EstadoPublished - 29 may 1981

Huella dactilar

Cibacron Blue F 3GA
RNA Polymerase I
Yeasts
Enzymes
Spectrophotometry
Chromatography
Catalytic Domain
Buffers
Coloring Agents
Salts
Adenosine Triphosphate
Peptides

ASJC Scopus subject areas

  • Medicine(all)

Citar esto

Bull, Paulina ; MacDonald, Heather ; Valenzuela, Pablo. / The interaction of yeast RNA polymerase I and Cibacron blue F3GA. En: BBA Section Nucleic Acids And Protein Synthesis. 1981 ; Vol. 653, N.º 3. pp. 368-377.
@article{139d79f8415e44f2ae86de668586b36f,
title = "The interaction of yeast RNA polymerase I and Cibacron blue F3GA",
abstract = "The interaction between yeast RNA polymerase I and Cibacron blue F3GA has been studied by difference spectrophotometry and column chromatography. The enzyme is reversibly inhibited by the dye. 50{\%} inhibition is obtained with 7.5 · 10-6 M Cibacron blue. 1 mol Cibacron blue binds per mol enzyme. This interaction, which is inhibited by salt, occurs at a site different from the active site. When RNA polymerase I is chromatographed in Blue dextran-Sepharose columns, two polypeptides, of 48 000 and 36 000 daltons, are dissociated from the enzyme. The resulting enzyme is completely inactive. ATP (5 mM) present in the elution buffer prevents both the dissociation of the polypeptides and the inactivation of the enzyme.",
author = "Paulina Bull and Heather MacDonald and Pablo Valenzuela",
year = "1981",
month = "5",
day = "29",
doi = "10.1016/0005-2787(81)90193-3",
language = "English",
volume = "653",
pages = "368--377",
journal = "BBA Section Nucleic Acids And Protein Synthesis",
issn = "0005-2787",
publisher = "Elsevier BV",
number = "3",

}

The interaction of yeast RNA polymerase I and Cibacron blue F3GA. / Bull, Paulina; MacDonald, Heather; Valenzuela, Pablo.

En: BBA Section Nucleic Acids And Protein Synthesis, Vol. 653, N.º 3, 29.05.1981, p. 368-377.

Resultado de la investigación: Article

TY - JOUR

T1 - The interaction of yeast RNA polymerase I and Cibacron blue F3GA

AU - Bull, Paulina

AU - MacDonald, Heather

AU - Valenzuela, Pablo

PY - 1981/5/29

Y1 - 1981/5/29

N2 - The interaction between yeast RNA polymerase I and Cibacron blue F3GA has been studied by difference spectrophotometry and column chromatography. The enzyme is reversibly inhibited by the dye. 50% inhibition is obtained with 7.5 · 10-6 M Cibacron blue. 1 mol Cibacron blue binds per mol enzyme. This interaction, which is inhibited by salt, occurs at a site different from the active site. When RNA polymerase I is chromatographed in Blue dextran-Sepharose columns, two polypeptides, of 48 000 and 36 000 daltons, are dissociated from the enzyme. The resulting enzyme is completely inactive. ATP (5 mM) present in the elution buffer prevents both the dissociation of the polypeptides and the inactivation of the enzyme.

AB - The interaction between yeast RNA polymerase I and Cibacron blue F3GA has been studied by difference spectrophotometry and column chromatography. The enzyme is reversibly inhibited by the dye. 50% inhibition is obtained with 7.5 · 10-6 M Cibacron blue. 1 mol Cibacron blue binds per mol enzyme. This interaction, which is inhibited by salt, occurs at a site different from the active site. When RNA polymerase I is chromatographed in Blue dextran-Sepharose columns, two polypeptides, of 48 000 and 36 000 daltons, are dissociated from the enzyme. The resulting enzyme is completely inactive. ATP (5 mM) present in the elution buffer prevents both the dissociation of the polypeptides and the inactivation of the enzyme.

UR - http://www.scopus.com/inward/record.url?scp=0019890629&partnerID=8YFLogxK

U2 - 10.1016/0005-2787(81)90193-3

DO - 10.1016/0005-2787(81)90193-3

M3 - Article

VL - 653

SP - 368

EP - 377

JO - BBA Section Nucleic Acids And Protein Synthesis

JF - BBA Section Nucleic Acids And Protein Synthesis

SN - 0005-2787

IS - 3

ER -