Abstract
A revised procedure for the purification of DNA-dependent RNA polymerase from H. halobium, including 2-phase parition, yields pure, highly active and absolutely DNA-dependent enzyme. Two forms of the enzyme, one containing, the other not containing a previously not observed component, .epsilon., show striking differences in activity. RNA polymerase without component .epsilon. has a significant activity on poly[d(A-T)] but only insignificant activity on all other templates. The enzyme containing a stoichiometric amount of component .epsilon. transcribes poly[d(A-T)] and native templates efficiently.