Single-strand-specific DNase activity is an inherent property of the 140-kDa protein of the snake venom exonuclease.
Polyclonal antibodies against the exonuclease from Crotalus adamanteus venom (the 140-kDa protein) inhibit both the exonucleolytic and the single-strand-specific endonucleolytic activities, present in the exonuclease preparation. The antibodies also diminish the ability of the enzyme to split the negatively supercoiled Bluescript KS+ in the AT-rich fragment near-by the transcription termination site of the Ampicillin gene. Therefore the single-strand-specific endonucleolytic activity was attributed to the protein molecule of the exonuclease. The processivity of the exonucleolytic action was found to be less than 3 monomers as indicated by the heparin trapping method.
Stoynov
S S
SS
Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia.
Bakalova
A T
AT
Dimov
S I
SI
Mitkova
A V
AV
Dolapchiev
L B
LB
D000818:Animals; D015153:Blotting, Western; D003435:Crotalid Venoms / Q000201:enzymology* / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism*; D003851:Deoxyribonucleases / Q000378:metabolism*; D005090:Exodeoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D006868:Hydrolysis; D008970:Molecular Weight; D013379:Substrate Specificity
D003435:Crotalid Venoms; D004277:DNA, Single-Stranded; D003851:Deoxyribonucleases; D005090:Exodeoxyribonucleases; C028450:exodeoxyribonuclease I