Single-strand-specific DNase activity is an inherent property of the 140-kDa protein of the snake venom exonuclease1

Autor:	Luben B. Dolapchiev, Svetoslav I. Dimov, Atanaska V. Mitkova, Anastassia T. Bakalova, Stoyno S. Stoynov
Rok vydání:	1997
Předmět:	chemistry.chemical_classification Exonuclease Biophysics Venom Cell Biology Processivity Biology Biochemistry Molecular biology Enzyme chemistry Structural Biology Snake venom Polyclonal antibodies Genetics biology.protein Molecular Biology Gene Klenow fragment
Zdroj:	FEBS Letters. 409:151-154
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
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::f6977ef7a8bbd5913c7a0373bc18333a https://doi.org/10.1016/s0014-5793(97)00489-4 Zobrazit plný text záznamu Plný text