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

FEBS Letters

Bakalova, Anastassia T¹  Mitkova, Atanaska V¹  Dolapchiev, Luben B¹  Stoynov, Stoyno S¹  Dimov, Svetoslav I¹ 

[1] Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria

关键词: Exonuclease;    Bluescript II KS+ plasmid;    Single-strand-specific endonuclease;    Processivity;    Crotalus adamanteus;    SVE;    snake venom exonuclease;    p-NPh.pT;    thymidin 5′-monophospho-p-nitrophenyl ester;    bis-p-NPhP;    bis-p-nitrophenyl phosphate;   

DOI  :  10.1016/S0014-5793(97)00489-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown