Summary
Arginase is an enzyme involved in the urea cycle and its deficiency results in argininemia, an autosomal recessive disorder accompanied by hyperammonemia. We isolated two overlapping cDNA clones and determined the entire nucleotide sequence (Haraguchiet al. 1987.Proc. Natl. Acad. Sci. USA 84: 412–415). Sequence analysis of eight cDNA clones revealed nucleotide variations at five positions in the protein coding region, and all these variations were accompanied by amino acid substitutions (Met to Lys at amino acid residue 1, Gln to Glu at residue 86, Ser to Phe at residue 109, Leu to Gln at residue 206, and Val to Ala at residue 233). These results suggest that human liver arginase is polymorphic in amino acid sequence, although some of the variations may be due to a transcription error or to cloning artifacts. Two restriction fragment length polymorphisms were identified at the arginase gene locus, using restriction endonucleasePvuII andHincII. These sequence polymorphisms and restriction fragment length polymorphisms may serve as linkage markers for arginase deficiency.
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Haraguchi, Y., Takiguchi, M., Matsuda, I. et al. Sequence heterogeneity of human liver arginase cDNAs and restriction fragment length polymorphism of the gene locus. Jap J Human Genet 33, 305–313 (1988). https://doi.org/10.1007/BF02032860
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DOI: https://doi.org/10.1007/BF02032860