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J. Biochem, 2003, Vol. 134, No. 5 711-718
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Molecular, Biochemical and Immunological Analyses of Canine Pancreatic DNase I

Yasushi Kaneko1,2, Haruo Takeshita1, Kouichi Mogi1, Tamiko Nakajima1, Toshihiro Yasuda3, Masako Itoi1, Hiroyuki Kuwano2 and Koichiro Kishi*,1

1 Department of Legal Medicine and Molecular Genetics, and 2 Department of General Surgical Science (Surgery I), Gunma University, Graduate School of Medicine, Maebashi, Gunma 371-8511; and 3 Department of Biology, Fukui Medical University, Matsuoka, Fukui 910-1193

The DNase I from canine pancreas was purified 260-fold to electrophoretic homogeneity with a 35% yield using three-step column chromatography. The activity of the purified enzyme was completely inhibited by 20 mM EDTA, an antibody specific to the purified enzyme and G-actin. A 1,373-bp cDNA encoding canine DNase I was constructed from the total canine pancreatic RNA using a rapid amplification of cDNA ends method, followed by sequencing. The mature canine DNase I protein was found to consist of 262 amino acids. A survey of DNase I in 13 different canine tissues revealed the highest levels of both DNase I enzyme activity and gene expression in the pancreas; therefore, the canine DNase I is of the pancreatic type. Phylogenetic and sequence identity analyses, studies of immunological properties and the tissue-distribution patterns of DNase I indicated that the canine enzyme is more closely related to the human DNase I than to other mammalian DNases I. Therefore, canine DNase I is found to be one of the best substitutes in studies of human DNase I.

* To whom correspondence should be addressed. Fax: +81-27-220-8035, E-mail: kkoichi{at}med.gunma-u.ac.jp


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