Title : Human genetically polymorphic
deoxyribonuclease : purification, characterization, and multiplicity of urine
deoxyribonuclease I
Abstract :
- A deoxyribonuclease I was purified from the urine of a 46-year-old male (a single individual) by using a series of column chromatographies to a homogeneous state as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
- The enzyme was found to be a glycoprotein , containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule
- The N-terminal amino acid sequence up to the 27th residue of the enzyme was similar to that of pancreatic deoxyribonuclease I from bovine and other species
- The catalytic properties of the enzyme derived from a single individual closely resembled those of deoxyribonuclease I purified from human urine collected from several volunteers [Ito, K. et al. (1984) J. Biochem
- 95, 1399-1406]
- The purified enzyme was found to consist of multiple forms with different pI values
- These findings are compatible with the existence of genetic polymorphism of deoxyribonuclease I in human urine previously reported [Kishi, K. et al. (1989) Hum
- Genet
- 81, 295-297]
- This multiplicity of the urine enzyme might be due to variations in the primary structure and/or differences in the content of sialic acid.