Isolation, purification and characterization of RNA polymerases from wheat germ

Autor: Jerome J. Jendrisak, Wayne M. Becker
Rok vydání: 1973
Předmět:
Zdroj: Biochimica et biophysica acta. 319(1)
ISSN: 0006-3002
Popis: Two DNA-dependent RNA polymerases (ribonucleoside triphosphate: RNA nucleotidyltransferase, EC 2.7.7.6) have been isolated from wheat germ. The enzymes were solubilized by high salt extraction with sonication and were resolved by DEAE-cellulose chromatography. Enzyme I eluted at 0.11 M (NH 4 ) 2 SO 4 , was insensitive to α-amanitin, and was relatively labile. Enzyme II eluted at 0.22 M (NH 4 ) 2 SO 4 , was inhibited by α-amanitin, and was stable after DEAE-cellulose chromatography. Both enzymes were more active with denatured than native DNA as template, but differed in their relative activities with Mg 2+ and Mn 2+ and in their ionic strength requirements. The quiescent wheat embryo appears to be a rich source of RNA polymerases and their properties are similar to nuclear RNA polymerases from other eukaryotes.
Databáze: OpenAIRE