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Publication : Molecular cloning and characterization of human and murine DNase II.

First Author  Baker KP Year  1998
Journal  Gene Volume  215
Issue  2 Pages  281-9
PubMed ID  9714827 Mgi Jnum  J:49551
Mgi Id  MGI:1277688 Doi  10.1016/s0378-1119(98)00280-7
Citation  Baker KP, et al. (1998) Molecular cloning and characterization of human and murine DNase II. Gene 215(2):281-9
abstractText  We have cloned and sequenced novel cDNAs that encode human and murine DNase II, the acidic deoxyribonuclease. Sequence analysis predicts that huDNase II contains an N-terminal signal sequence and that mature DNase II has 344 residues with a calculated molecular mass of 38 032 Da. DNase II is a novel enzyme with no homologies to proteins of known function. Surprisingly, C. elegans appears to possess a family of DNase II homologs. Unlike DNase I-like enzymes that have tissue-specific expression patterns, huDNase II is ubiquituously expressed at low levels. When huDNase II is expressed in human 293 cells, we observe secretion of a novel 42-44 kDa glyco-protein; approximately 20-30% of recombinant human DNase II activity is secreted in this system. The secreted enzyme possesses DNA hydrolytic activity and shares biochemical properties with purified DNase II obtained from other species. We also show that the mechanism by which DNase II cuts DNA is similar to DNase I in that the enzyme produces nicks rather than double-strand cuts.
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