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| 【主 题】 ： |
Native Bovine Deoxyribonuclease I |
| 【联系人名】 ： |
Lisa Clara |
| 【电子邮件】 ： |
contact@creative-enzymes.com |
| 【联系电话】 ： |
15166698109 |
| 【发布日期】 ： |
2016-8-27 |
| 【详细说明】 ： |
DNase I is an endonuclease that acts on
phosphodiester bonds adjacent to pyrimidines to
produce polynucleotides with terminal 5′-
phosphates. In the presence of Mg2+, DNAse I cleaves
each strand of DNA independently and the cleavage
sites are random. Both DNA strands are cleaved at
approximately the same site in the presence of
Mn2+.2 The pH optimum is found to be between 7 and
8. Divalent cations such as Mn2+, Ca2+, Co2+, and
Zn2+ are activators of the enzyme.3 A concentration
of 5 mM Ca2+ stabilizes the enzyme against
proteolytic digestion. DNAse I from bovine pancreas
consists of four chromatographically distinguishable
components, A, B, C, and D, with molar ratios being
4:1:1 respectively. Only minor amounts of D are
found.4 2-Mercaptoethanol, chelators, sodium dodecyl
sulfate (SDS)5 and actin6 are known to inhibit the
enzyme activity.
http://www.creative-enzymes.com/product/Native-
Bovine-Deoxyribonuclease-I_1725.html
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English
