Of all arginine catabolic enzymes, the arginases and nitric oxide (NO) synthases are the
ones that are of greatest interest to many investigators. Mammalian arginases catalyze the …

Background: Nitric oxide (NO) is a biomediator believed to be synthesized primarily from
extracellular arginine. Various methodologies have been used to inhibit NO synthesis so as …

Arginine is one of the most versatile amino acids in animal cells, serving as a precursor for
the synthesis not only of proteins but also of nitric oxide, urea, polyamines, proline …

A new radiometric assay for the enzyme arginase has been developed, depending on the
conversion of 14C-guanidoarginine to 14C-urea and cleavage of the latter to 14CO2 by …

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 …

The arginase enzyme developed in early life forms and was maintained during evolution. As
the last step in the urea cycle, arginase cleaves l-arginine to form urea and l-ornithine. The …

ABSTRACT L-Arginine is the biological precursor of nitric oxide (NO), which serves as an
important signal and effector molecule in animals. This review summarizes some structure …

An assay for arginase is described that uses l-[guanido-14C] arginine as substrate.
Unhydrolyzed arginine is removed in a batch procedure with sulfonate resin and the [14C] …

Summary Arginase (EC 3.5. 3.1), the final enzyme in the urea cycle, catalyzes the cleavage
of arginine to orthinine and urea. At least two forms of this enzyme, Al and All, have been …

Mammalian liver arginase is a trimeric enzyme that contains a Mn2–Mn2 cluster in each
active site (1–3). Arginase catalyzes the hydrolysis of L-arginine to form L-ornithine and …