Arginase exists in two isoforms. Liver-type arginase (arginase I) is expressed almost
exclusively in the liver and catalyzes the last step of urea synthesis, whereas the nonhepatic …

Liver-type arginase (arginase I) is expressed almost exclusively in the liver and catalyzes
the last step of urea synthesis, whereas the nonhepatic type (arginase II) is expressed in …

Nitric oxide (NO) is synthesized from arginine by nitric-oxide synthase (NOS), and citrulline
that is generated can be recycled to arginine by argininosuccinate synthase (AS) and …

Human type II arginase, which is extrahepatic and mitochondrial in location, catalyzes the
hydrolysis of arginine to form ornithine and urea. While type I arginases function in the net …

Experiments were performed to identify arginase isoforms expressed in primary and
transformed rodent macrophages and to determine the molecular mechanisms for the …

There are two forms of arginase in humans, both catalyzing the hydrolysis of arginine to
ornithine and urea. Recent studies in animal models and in Type I arginase-deficient …

Partial cloning and characterization of an arginine decarboxylase in the kidney. Using
homology-based polymerase chain reaction (PCR) amplification, we demonstrate the …

Arginase exists in two isoforms, the hepatic (arginase I) and extrahepatic types (arginase II).
Arginase I is markedly induced in rat peritoneal macrophages and rat tissues in vivo by …

Arginine is a precursor for the synthesis of urea, polyamines, creatine phosphate, nitric oxide
and proteins. It is synthesized from ornithine by argininosuccinate synthetase and …

Macrophages can express two arginase isoforms with distinct subcellular localization
(cytosolic AI and mitochondrial AII). These isoforms are products of different genes and are …