Functional characterization of a human DNase-like protein encoded by a gene positioned in Xq28
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- 作者：Appierto ; Valentina ; Bardella ; Lidia ; Vijayasarathy ; C. ; Avadhani ; Narayan ; Sgaramella ; Vittorio ; et. al.
- 关键词：Endonuclease ; Acidic DNase ; Human chromosome X ; aa ; amino acid (s) ; IPTG ; isopropyl β ; -d-thiogalactoside ; MBP ; maltose binding protein ; MBS ; N-maleimidobenzoyl N-hydroxysuccinimide ester ; PBS ; phosphate-buffered saline ; SDS ; sodium dodecyl sulphate ; X
- 刊名：Gene
- 出版年：1997
- 出版时间：March 25, 1997
- 年：1997
- 卷：188
- 期：1
- 页码：119-122
- 全文大小：129 K
文摘
Xib, a gene recently reported to reside on the q28 region of the human X chromosome [Pergolizzi et al. (1996) Gene 168, 267–270], contains an open reading frame homologous to those of the DNase I family enzymes. The full open reading frame of this gene has been fused to the E. coli gene of the maltose binding protein and expressed in bacteria as a chimeric protein. The partially purified chimeric protein is enzymatically active. It introduces single and double stranded breaks into supercoiled DNA, at 30°C in the absence of divalent cations and at a pH optimum of 5.2. To our knowledge this enzyme represents the first cloned human endonuclease with characteristics similar to those of acidic DNase II.