RNA-dependent DNA polymerase activity of RNA tumor virus. VI. Processive mode of action of avian myeloblastosis virus polymerase.


Purified avian myeloblastosis virus (AMV) polymerase consisting of alpha,beta subunits has been shown to act processively in catalyzing DNA synthesis primed with 34S AMV RNA oligo(dT), poly(A)-poly(dT), and poly(I)-poly(dC). DNA transcripts prepared with 34S AMV RNA-oligo(dT)14 and AMV polymerase (alphabeta) have been shown to have a molecular weight of 1.05 X 10(6), or approximately one-third the size of the 34S RNA genome. Polymerase subunit alpha acts nonprocessively with the above templates.




Reverse Transcriptase, Historical Protein Properties (MW, pI, ...), Source / Purification, RNase H Activity, Kinetic Parameters


new topics/pols set partial results complete validated


Polymerase Reference Property Result Context
AMV Leis JP1976 Reverse Transcriptase Activity Yes
AMV Leis JP1976 Molecular Weight 1.73E+05 Dalton
AMV Leis JP1976 Cloned or native Native organism
AMV Leis JP1976 Tagged No
AMV Leis JP1976 Full length or truncated Full length
AMV Leis JP1976 RNase H Yes
AMV Leis JP1976 KM 10uM Reaction: Nucleotide incorporation; Substrate: dNTPs

Entry validated by:

Log in to edit reference All References

Using Polbase tables:


Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).


It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.