Arginine:glycine amidinotransferase. A comparative study in lizard and mouse tissues.
Kidney transamidinase activity in the lizard (Calotes versicolor), like that in the mouse, showed the pH optimum at 7.4. The lizard enzyme was inhibited to a greater degree than the mouse enzyme at high concentrations (greater than 20 mM) of L-arginine and glycine. Kidney and liver in the lizard and kidney and pancreas in the mouse were the tissues with high transamidinase activity. While transamidinase activity was widely distributed in mouse tissues, the enzyme was found to be restricted only to a few tissues in the lizard. Hydrocortisone administration into male lizards did not significantly alter the transamidinase levels in kidney and liver.
D000579:Amidinotransferases / Q000378:metabolism*; D000818:Animals; D006854:Hydrocortisone / Q000494:pharmacology; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008116:Lizards / Q000378:metabolism*; D008297:Male; D051379:Mice
D000579:Amidinotransferases; C020681:glycine amidinotransferase; D006854:Hydrocortisone