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DNase I cleaves DNA to form two oligonucleotide-end products with 5’-phospho and 3’-hydroxy ends and is produced mainly by organs of the digestive system. The DNase I family requires Ca2+ and Mg2+ cations as activators and selectively expressed. [1] In terms of pH, the DNAses I family is active in normal pH of around 6.5 to 8.
Deoxyribonuclease I (usually called DNase I), is an endonuclease of the DNase family coded by the human gene DNASE1. [5] DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides.
Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes.
Type I site-specific deoxyribonuclease (EC 3.1.21.3, type I restriction enzyme, deoxyribonuclease (ATP- and S-adenosyl-L-methionine-dependent), restriction-modification system, deoxyribonuclease (adenosine triphosphate-hydrolyzing), adenosine triphosphate-dependent deoxyribonuclease, ATP-dependent DNase, type 1 site-specific deoxyribonuclease) is an enzyme. [1]
In molecular biology, endonucleases are enzymes that cleave the phosphodiester bond within a polynucleotide chain (namely DNA or RNA).Some, such as deoxyribonuclease I, cut DNA relatively nonspecifically (with regard to sequence), while many, typically called restriction endonucleases or restriction enzymes, cleave only at very specific nucleotide sequences.
b. DNase (Deoxyribonuclease): DNase degrades DNA present in the lysate, reducing its viscosity and preventing DNA-related interference in downstream purification steps. c. RNase (Ribonuclease): Similar to DNase, RNase degrades RNA in the lysate, reducing its viscosity and minimizing RNA-related interference.
Deoxyribonuclease II (EC 3.1.22.1, DNase II, pancreatic DNase II, deoxyribonucleate 3'-nucleotidohydrolase, pancreatic DNase II, acid deoxyribonuclease, acid DNase) is an endonuclease that hydrolyzes phosphodiester linkages of deoxyribonucleotide in native and denatured DNA, yielding products with 3'-phosphates and 5'-hydroxyl ends, which occurs as a result of single-strand cleaving mechanism. [1]
Each nucleotide in RNA contains a ribose sugar, with carbons numbered 1' through 5'. A base is attached to the 1' position, in general, adenine (A), cytosine (C), guanine (G), or uracil (U). Adenine and guanine are purines, and cytosine and uracil are pyrimidines. A phosphate group is attached to the 3' position of one ribose and the 5 ...