Cloning and characterization of the mouse and rat type II arginase genes

Ramaswamy K. Iyer, Joanne M. Bando, Christopher P. Jenkinson, Joseph G. Vockley, Phillip S. Kim, Rita M. Kern, Stephen D. Cederbaum, Wayne W. Grody

Research output: Contribution to journalArticlepeer-review

35 Scopus citations


Two forms of arginase, both catalyzing the hydrolysis of arginine to ornithine and urea, are found in animals ranging from amphibians to mammals. In humans, inherited deficiency of hepatic or type I arginase results in hyperargininemia, a syndrome characterized by periodic episodes of hyperammonemia, spasticity, and neurological deterioration. In these patients, a second extrahepatic or type II arginase activity is significantly increased, an induction that may partially compensate for the lack of AI activity and apparently mitigates some of the clinical effects of the condition. Cloning and characterization of the human AII cDNA was recently accomplished. The cloning, sequencing, and partial characterization of the mouse and rat AII cDNAs are reported herein. The DNA sequences predicted polypeptides of 354 amino acids, including a N-terminal mitochondrial import signal. Sequence homology to the human type II arginase, arginase activity data, and immunoprecipitation with an anti-AII antibody confirm the identity of these cloned genes as rodent extrahepatic type II arginases.

Original languageEnglish (US)
Pages (from-to)168-175
Number of pages8
JournalMolecular Genetics and Metabolism
Issue number3
StatePublished - Mar 1998
Externally publishedYes


  • Arginase
  • In vitro expression
  • Phylogeny
  • Urea cycle

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Endocrinology


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