| First Author | Mori S | Year | 2001 |
| Journal | Biochim Biophys Acta | Volume | 1547 |
| Issue | 2 | Pages | 275-87 |
| PubMed ID | 11410284 | Mgi Jnum | J:70161 |
| Mgi Id | MGI:2136521 | Doi | 10.1016/s0167-4838(01)00196-0 |
| Citation | Mori S, et al. (2001) Molecular, biochemical and immunological analyses of porcine pancreatic DNase I. Biochim Biophys Acta 1547(2):275-87 |
| abstractText | Deoxyribonuclease I (DNase I) was purified 26500-fold in 39% yield from porcine pancreas to electrophoretic homogeneity using three-step column chromatography. The purified enzyme was inhibited by an antibody specific to the purified enzyme but not by G-actin. A 1303 bp cDNA encoding porcine DNase I was constructed from total RNA from porcine small intestine using a rapid amplification of cDNA ends method, followed by sequencing. Mature porcine DNase I protein was found to consist of 262 amino acids. Unlike all other mammalian DNase I enzymes that are inhibited by G-actin, porcine DNase I has H65 and S114 instead of Y65 and A114, which presumably results in the lack of inhibition. Porcine DNase I was more sensitive to low pH than rat or bovine enzymes. Compared with their primary structures, the amino acid at position 110 was N in porcine enzyme, but S in rat and bovine enzymes. A porcine mutant enzyme in which N was substituted by S alone at position 110 (N110S) became resistant to low pH to a similar extent as the rat and bovine enzymes. |
