The Catalytic Properties of Human Hepatitis B Virus Polymerase
β Scribed by Ji Hoon Jeong; Dong Seok Kwak; Hyune Mo Rho; Guhung Jung
- Book ID
- 115578572
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 744 KB
- Volume
- 223
- Category
- Article
- ISSN
- 0006-291X
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## Abstract A soluble DNA polymerase was purified 8,000βfold from hepatitis B surface antigen positive serum. The molecular weight of the enzyme by gel filtration was about 1.60 Γ 10^5^, the sedimentation coefficient was 5.5S, the apparent Km for dTTP was 4 MM, the optimum pH in the presence of Mg^
Human hepatitis B virus (HBV) DNA polymerase activity was inhibited by pyridoxal 5'-phosphate (PLP) specifically and noncompetitively with respect to deoxythymidine triphosphate (dTTP). NaBH, reduction of PLP-HBV core proteins resulted in the complete inactivation of HBV DNA polymerase, and PLP modi