Soluble Rous sarcoma virus reverse transcriptases α, αβ, and β purified from insect cells are processive DNA polymerases that lack an RNase H 3' → 5' directed processing activity

Journal of Biological Chemistry

Volumn 274, Issue 37, 1999, Pages 26329-26336

  Werner, Susanne ^a   Wöhrl, Birgitta M ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA POLYMERASE; RIBONUCLEASE H; RNA; RNA DIRECTED DNA POLYMERASE;

ARTICLE; ENZYME MECHANISM; ENZYME POLYMORPHISM; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SUBUNIT; INSECT; MOLECULAR CLONING; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; RNA PROCESSING; ROUS SARCOMA ONCOVIRUS; VIRUS REPLICATION;

ANIMALS; AVIAN SARCOMA VIRUSES; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DNA-DIRECTED DNA POLYMERASE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROLYSIS; ISOENZYMES; PROTEIN CONFORMATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT PROTEINS; RIBONUCLEASE H, CALF THYMUS; RNA-DIRECTED DNA POLYMERASE; SPODOPTERA;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; INSECTA; ONCOVIRINAE; RICE STRIPE VIRUS; ROUS SARCOMA VIRUS;

EID: 0039701536     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.37.26329     Document Type: Article

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