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J Biol Chem, Vol. 273, Issue 27, 17192-17198, July 3, 1998

Porcine Spleen Deoxyribonuclease II
COVALENT STRUCTURE, cDNA SEQUENCE, MOLECULAR CLONING, AND GENE EXPRESSION

Cheng-Ching Wang, Shao-Chun Lu, Hui-Ling Chen^§, and Ta-Hsiu Liao

From the  Institute of Biochemistry and ^§ Hepatitis Research Center, College of Medicine, National Taiwan University, Taipei, Taiwan

Porcine spleen DNase II, a lysosomal acid hydrolase, is a noncovalently linked · heterodimer (Liao, T.-H. (1985) J. Biol. Chem. 260, 10708-10713). The  subunit, after disulfide cleavage, yields two chains, 1 and 2. The complete amino acid sequences of the 1, , and 2 chains were elucidated by protein sequencing, and the pairings of one interchain disulfide between 1 and 2 and of three intrachain disulfides in 2 were assigned. Six carbohydrate attachment sites, two in  and four in 2, were detected by sugar analyses. The cDNA of DNase II was amplified using primers synthesized on the basis of the amino acid sequences determined. The amplified fragments shown to be a cDNA sequence of 1,292 bases. This cDNA sequence has an open reading frame encoding a 364-amino acid polypeptide containing a putative transmembrane peptide at the NH₂-end, two small connecting peptides in the middle, and a peptide at the COOH terminus. These are evidently removed to form mature DNase II. Thus, all three chains in the sequence 1, , and 2 are coded by the same cDNA. When Chinese hamster ovary cells were transfected with a cloned plasmid with an inserted cDNA fragment encoding the entire reading frame, the expressed protein was released into the growth medium as an active form of DNase II.

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