Die Isolierung eines Amatoxin-bindenden Proteins, das von der RNA-Polymerase B und C verschieden ist
- 1 January 1976
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 357 (1) , 89-94
- https://doi.org/10.1515/bchm2.1976.357.1.89
Abstract
During the isolation of the amatoxin RNA-polymerase B-complex from calf thymus tissue, a protein (ABP) was isolated which shows such strong affinity to [3H]amanin that significant binding occurs at low concentrations (10-7 M) of the label. The presence of a new amatoxin-complex is demonstrated by coprecipitation of amatoxin and ABP with ammonium sulfate and common chromatography on phosphocellulose and Sephadex G-25. The new protein ABP is characterized by denaturating sodium dodecylsulfate-gel electrophoresis. The molecular masses of both main bands, possibly subunits of ABP, are determined as 100,000 and 10,000-15,000 daltons and different from the subunit pattern of RNA-polymerases B and C.This publication has 1 reference indexed in Scilit:
- Multiple RNA polymerase species from rat liver tissue: Possible existence of a cytoplasmic enzymeArchives of Biochemistry and Biophysics, 1972