Abstract
Human placental extracts contain a specific inhibitor of mammalian retroviral RNA-directed DNA polymerase (deoxynucleosidetriphosphate:DNA deoxynucleotidyltransferase, EC 2.7.7.7) activity. This inhibitor copurifies with retrovirus-like particles in human placental extracts. The inhibitor can be removed from these particles by salt extraction, which leads to the recovery of the polymerase activity. Thus, the inhibitor does not irreversibly inactivate the particle-associated RNA-directed DNA polymerase activity. The inhibitory preparation contained no nuclease, protease, or phosphatase activity. Because its inhibitory action can be eliminated by the addition of more virus to the reaction, nonspecific inactivation of enzyme substrate has been ruled out. A partial characterization of the inhibitor indicates that it is (i) insensitive to ether, trypsin, and phospholipase C; (ii) stable to heat and pH 2-12; and (iii) nondialyzable.
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