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Single‐strand‐specific DNase activity is an inherent property of the 140‐kDa protein of the snake venom exonuclease 1
Author(s) -
Stoynov Stoyno S,
Bakalova Anastassia T,
Dimov Svetoslav I,
Mitkova Atanaska V,
Dolapchiev Luben B
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00489-4
Subject(s) - venom , exonuclease , chemistry , deoxyribonucleases , deoxyribonuclease i , snake venom , hypersensitive site , biochemistry , microbiology and biotechnology , biology , enzyme , dna , base sequence , polymerase
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.