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Solubilized DNA‐dependent RNA polymerase from human placenta: A Mn 2+ ‐dependent enzyme
Author(s) -
Voigt H.-P.,
Kaufmann R.,
Matthaei H.
Publication year - 1970
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(70)80642-1
Subject(s) - solubilization , chemistry , enzyme , placenta , dna , microbiology and biotechnology , polymerase , rna , human placenta , biochemistry , biophysics , biology , fetus , gene , genetics , pregnancy
The 100‐fold purified RNA polymerase activity from human placenta is completely dependent upon added DNA. The enzyme is most active at 3 mM Mn 2+ in the presence of 100 mM (NH 4 ) 2 SO 4 . Denatured DNA is a better template than native DNA. α‐Amanitin completely inhibits the incorporation of 3 H‐UMP, while rifampicin has no influence upon the enzymatic activity.