Identification of the three non‐identical subunits constituting human deoxyribonuclease II

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Abstract
We purified DNase II from human liver to apparent homogeneity. The N‐terminal amino acid sequences of each of three components constituting the purified mature enzyme were then separately determined by automatic Edman degradation. A combination of this chemical information and the previously reported nucleotide sequence of the cDNA encoding human DNase II [Yasuda et al. (1998) J. Biol. Chem. 273, 2610–2626] allowed detailed elucidation of the enzyme's subunit structure: human DNase II was composed of three non‐identical subunits, a propeptide, proprotein and mature protein, following a signal peptide. Expression analysis of a series of deletion mutants derived from the cDNA of DNase II in COS‐7 cells suggested that although a single large precursor protein may not be necessary for proteolytic maturation, the propeptide region L17–Q46 may play an essential role in generating the active form of the enzyme.

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