Abstract

We investigated the inhibitory effects of aurochloric acid (AuCl4H) on reverse transcriptase (RT) derived from avian myeloblastosis virus and DNA polymerase a (pol. a) purified from HeLa S3 cells. The activities of RT, pol. a and E. coli DNA polymerase I (pol. I) with dTTP as the substrate were inhibited 50% at AuCl4H concentrations of 18 μM, 43 μM and 230 μM, respectively. AuCl4H inhibited RT activity competitively with respect to the substrate, dTTP, and uncompetitively with the template/primer, (rA)n(dT)12‐18. In assays with dGTP as the substrate, 50% inhibitions of RT, pol. a and pol. I activities were observed at AuCl4H concentrations of 100 μM, 450 μM and 580 μM, respectively. AuCl4H inhibited RT activity uncompetitively with respect to the substrate, dGTP, and noncompetitively with the template/primer, (rC)n(dG)12‐18. AuCl4H at concentrations causing more than 50% inhibition of RT activity had little inhibitory effect on the colony‐forming ability of HeLa cells or their syntheses of DNA, RNA and protein.

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