Reverse Transcriptase Associated with Avian Sarcoma-Leukosis Viruses. II. Comparison of Subunit Structure and Catalytic Properties

The three enzyme forms (=-, =β and β-form) of the RNA-dependent DNA polymerase (the reverse transcriptase) from three strains of avian sarcoma virus (ASV B77, ASV tsLA334, and ASV QV2) and one exogenous (avian myeloblastosis virus (AMV)) and one endogenous avian leukosis virus (Rous-associated virus...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1982-01, Vol.91 (1), p.323-330
Main Authors: UENO, Akemichi, ISHIHAMA, Akira
Format: Article
Language:English
Subjects:
Alpharetrovirus - enzymology
Animals
Avian Leukosis Virus - enzymology
Avian Myeloblastosis Virus - enzymology
Cells, Cultured
Chick Embryo
Coturnix
Endopeptidases
Fibroblasts
Macromolecular Substances
Molecular Weight
Oligodeoxyribonucleotides - metabolism
Poly G - biosynthesis
Poly T - biosynthesis
RNA-Directed DNA Polymerase - metabolism
Serine Endopeptidases
Substrate Specificity
Temperature
Templates, Genetic
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Summary:The three enzyme forms (=-, =β and β-form) of the RNA-dependent DNA polymerase (the reverse transcriptase) from three strains of avian sarcoma virus (ASV B77, ASV tsLA334, and ASV QV2) and one exogenous (avian myeloblastosis virus (AMV)) and one endogenous avian leukosis virus (Rous-associated virus type-0 (RAV-0)) were compared with each other in subunit structure and catalytic properties. Despite the gross similarity in the subunit molecular weight (Mr(α)=65,000 and Mrβ=92,000), minor differences were found in the molecular size of the subunit as determined by SDS-gel electrophoresis, the order being ASV tsLA334≤ASV QV2
ISSN:0021-924X
DOI:10.1093/oxfordjournals.jbchem.a133691