Purification and characterization of genetically polymorphic deoxyribonuclease I from human kidney.
Deoxyribonuclease I (DNase I) was purified about 850,000-fold from human kidney using a rabbit anti-human urine DNase I antibody and sensitive DNase I activity assay. On SDS-PAGE, the purified kidney DNase I gave a single major band, and its molecular mass was estimated to be 38,000 Da. The activity of purified kidney DNase I was dependent on the presence of Mg2+ and Ca2+. G-Actin inhibited the activity, as did the anti-urine DNase I antibody. The properties of the kidney DNase I were the same as those of urine DNase I.
Nadano
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D
Department of Legal Medicine, Fukui Medical School.
Yasuda
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T
Kishi
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K
D000199:Actins / Q000494:pharmacology; D000328:Adult; D002850:Chromatography, Gel / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D003850:Deoxyribonuclease I / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D011110:Polymorphism, Genetic
D000199:Actins; D003850:Deoxyribonuclease I