Properties of Hepatitis B Virus Associated DNA Polymerase.
10.3349/ymj.1985.26.2.175
- Author:
Sang Hwan OH
1
;
Yean Hee PARK
Author Information
1. Department of Biochemistry, College of Medicine, Yonsei University, Seoul, Korea.
- Publication Type:Original Article
- Keywords:
HBV-DNA polymerase;
PFA;
ara-ATP;
ara-CTP
- MeSH:
DNA-Directed DNA Polymerase/antagonists & inhibitors;
DNA-Directed DNA Polymerase/metabolism*;
Hepatitis B Virus/enzymology*;
Human
- From:Yonsei Medical Journal
1985;26(2):175-183
- CountryRepublic of Korea
- Language:English
-
Abstract:
The nature of hepatitis B virus (HBV) particle associated DNA polymerase was studied in relation to various enzyme inhibitors including antiviral agents. HBV DNA polymerase required high concentration of MgCl2(> 30 mM) and neutral pH for its full activity. p-chloromercuribenzoate was a strong inhibitor (85% inhibition at 1 mM) but N-ethylmaleimide had much less inhibitory effect (20% inhibition at 10 mM). Phosphonoformic acid showed the greatest inhibitory effect on HBV-DNA polymerase (almost complete inhibition at 100 microM) among phosphocompounds tested. Adenine arabinoside triphosphate (ara-ATP) and cytosine arabinoside triphosphate (ara-CTP) were competitive inhibitors with respect to their respective deoxyribonucleoside triphosphate (dATP and dCTP). Ara-CPT was a stronger inhibitor of HBV-DNA polymerase compared to ara-ATP. Ki values for ara-ATP and ara-CTP were 15.0 microM and 11.7 microM , respectively. HBV-DNA polymerase is characteristic in its ionic requirements and susceptibilities to certain inhibitors.
