Single-strand-specific DNase activity is an inherent property of the 140-kDa protein of the snake venom exonuclease 1Enzymes: snake venom exonuclease (oligonucleate 5′-nucleotidohydrolase, EC 3.1.15.1).1

Autor: Stoynov, Stoyno S, Bakalova, Anastassia T, Dimov, Svetoslav I, Mitkova, Atanaska V, Dolapchiev, Luben B
Jazyk: angličtina
Předmět:
Zdroj: FEBS Letters. (2):151-154
ISSN: 0014-5793
DOI: 10.1016/S0014-5793(97)00489-4
Popis: 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.
Databáze: OpenAIRE