Studies on the advent of ureotelism. Factors that render the hepatic arginase of the Mexican axolotl able to hydrolyse endogenous arginine.
1. A study was undertaken of the conditions that might operate in the synthesis and hydrolysis of arginine by axolotl liver homogenate to test a previous postulate that liver arginase of the non-metamorphosed Mexican axolotl is not able to hydrolyse arginine formed from citrulline and aspartic acid, though it can split exogenous arginine, and also that an enhanced capacity to hydrolyse endogenous arginine plays a major role in the advent of ureotelism observed during the metamorphosis of the axolotl. 2. It was found that the arginase from axolotl liver is very unstable under the conditions followed, contrary to what is observed in rat liver. 3. Axolotl arginase is able to hydrolyse endogenous arginine if preserved. 4. Mn(2+) protects the enzyme and renders it able to split endogenous arginine. 5. It is suggested that the metal ion produces a change of conformation of the enzyme that, being stable, is capable of hydrolysing the amino acid, or that the new conformation is appropriate for interaction with the sites of arginine synthesis.
D000818:Animals; D001119:Arginase / Q000378:metabolism*; D001120:Arginine / Q000096:biosynthesis / Q000378:metabolism*; D001224:Aspartic Acid / Q000378:metabolism; D002956:Citrulline / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008345:Manganese; D008675:Metamorphosis, Biological; D014562:Caudata
D002956:Citrulline; D001224:Aspartic Acid; D008345:Manganese; D001120:Arginine; D001119:Arginase