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Comparative Study
. 1997 Oct 1;346(1):15-20.
doi: 10.1006/abbi.1997.0275.

Purification, characterization, and amino acid sequencing of DNase gamma from rat spleen

Affiliations
Comparative Study

Purification, characterization, and amino acid sequencing of DNase gamma from rat spleen

D Shiokawa et al. Arch Biochem Biophys. .

Abstract

An endonuclease named DNase gamma was purified to apparent homogeneity from rat splenocyte nuclei and its properties were characterized. We also determined the NH2-terminal and partial amino acid sequences of the proteolytic internal peptides. The molecular mass of gamma DNase was 33,000 daltons as determined by SDS-polyacrylamide gel electrophoresis. A native molecular mass of 30,000 was estimated by gel filtration. Purified DNase gamma is active in the presence of both Ca2+ and Mg2+ or Mn2+ alone and inhibited by Co2+, Ni2+, Cu2+, and especially Zn2+. Maximal activity was achieved at pH 7.2 in Mops-NaOH buffer. The sequence data on the NH2-terminal and seven internal peptides obtained by sequential digestions with Achromobacter protease I and endoproteinase Asp-N revealed that DNase gamma is a novel endonuclease that shows sequence homology with DNase I.

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