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1: Biochem Biophys Res Commun. 1999 Jun 24;260(1):280-3.Click here to read Links

A new allele, DNASE1*6, of human deoxyribonuclease I polymorphism encodes an Arg to Cys substitution responsible for its instability.

Yasuda T, Takeshita H, Iida R, Kogure S, Kishi K.

Department of Legal Medicine, Gunma University School of Medicine, Maebashi, 371-8511, Japan.

A new allele, DNASE1*6, of human deoxyribonuclease I (DNase I) has been discovered by isoelectric focusing: its gene product has the most cathodic pI of the six electrophoretic variants. Results of DNA sequencing, mismatched PCR-restriction fragment length polymorphism, and transient transfection of the variant construct showed that the mutant was caused by a C-T transition at nucleotide position 1826, resulting in an Arg to Cys substitution at amino acid position 185 of the mature enzyme. The variant isoenzyme, expressed in COS-7 cells, was more labile than the other types. Instability and an increase in the pI value of the variant suggest that a structural alteration, perhaps due to aberrant formation of a disulfide bond, could occur in the enzyme. Copyright 1999 Academic Press.

PMID: 10381379 [PubMed - indexed for MEDLINE]