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J. Biochem, 1980, Vol. 87, No. 4 1097-1103
© 1980 Japanese Biochemical Society

research-article

Purification and Properties of Deoxyribonuclease II from Human Urine

Koichiro MURAI1, Masayoshi YAMANAKA, Kimihiro AKAGI and Motoaki ANAI2

Second Department of Internal Medicine, Faculty of Medicine, Kyushu University 60 Higashi-ku, Fukuoka, Fukuoka 812

1To whom correspondence should be addressed.

The acid deoxyribonucleases [DNase II; EC 3.1.4.6 [EC] ] in human urine were purified approximately 400- to 500-fold by phosphocellulose chromatography, gel filtration on Sephadex G-75 and isoelectric focusing, with a total recovery of 22%.

The enzymes were present in at least three forms with different isoelectric points, pHs 6.4, 6.6, and 6.8. However, other properties were essentially similar. The enzymes did not require divalent cations for activity, and the optimal pHs were at 5.1 to 5.3 in 33 mM acetate buffer. They had a molecular weight of around 36,000, as estimated by gel filtration on Sephadex G-75. The enzymes were endonucleases which hydrolyzed native, double-stranded DNA about 5 to 15 times faster than thermally denatured DNA. The products formed from native DNA were 3'-phosphoryl- and 5'-hydroxyl-terminated oligonucleotides. The average chain length of the limit digests with these enzymes was approximately 11 to 15, and the major fragments were longer than pentanucleotides. The final preparations were free of nonspecific acid and alkaline phosphatases and phosphodiesterase, but contained contaminating ribonuclease activity.

2Present address: Department of Medical Technology, School of Health Sciences, Kyushu University, Fukuoka, Fukuoka 812.


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