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Literature summary for 2.7.7.49 extracted from

  • Hansen, J.; Schulze, T.; Moelling, K.
    RNase H activity associated with bacterially expressed reverse transcriptase of human T-cell lymphotropic virus III/lymphadenopathy-associated virus (1987), J. Biol. Chem., 262, 12393-12396.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Human T-cell lymphotropic virus/lymphadenopathy-associated virus

General Stability

General Stability Organism
stable against freezing, thawing, overnight dialysis and high dilutions Human T-cell lymphotropic virus/lymphadenopathy-associated virus

Organism

Organism UniProt Comment Textmining
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Human T-cell lymphotropic virus/lymphadenopathy-associated virus

Storage Stability

Storage Stability Organism
-20°C, 50% glycerol, stable Human T-cell lymphotropic virus/lymphadenopathy-associated virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn
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Human T-cell lymphotropic virus/lymphadenopathy-associated virus diphosphate + DNAn+1
-
?

Subunits

Subunits Comment Organism
More two polypeptides of 66000 Da and 41000 Da are detectable in polymerase-expressing bacterial lysates. The 51000 Da protein appears to originate from the 66000 Da molecule Human T-cell lymphotropic virus/lymphadenopathy-associated virus