[Isolation of an amatoxin binding protein (ABP) different from RNA-polymerase B and C ((author's transl))].
During the isolation of the amatoxin RNA-polymerase B-complex from calf thymus tissue we also isolated a protein (ABP) which shows such strong affinity to [3H)amanin that significant binding occurs at low concentrations (10-7M) of the label. The presence of a new amatoxin-complex is demonstrated by coprecipitation of amatoxin and ABP with ammonium sulphate and the common chromatography on phosphocellulose and Sephadex G-25. The new protein ABP is characterized by denaturating sodium dodecylsulphate-gel electrophoresis. The molecular masses of both main bands - possibly subunits of ABP - are determined as 100000 and 10000 - 15000 Dalton and different from the subunit pattern of RNA-polymerases B and C.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D011485:Protein Binding; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism; D011955:Receptors, Drug; D013950:Thymus Gland / Q000201:enzymology; D014118:Toxins, Biological / Q000378:metabolism*
D011506:Proteins; D011955:Receptors, Drug; D014118:Toxins, Biological; D012321:DNA-Directed RNA Polymerases
Die Isolierung eines Amatoxin-bindenden Proteins, das von der RNA-Polymerase B und C verschieden ist