Leucine aminopeptidase in extracts of swine muscle.
1. Leucine aminopeptidase (EC 3.4.1.1) has been demonstrated in swine muscle at a level of activity one-fifth that of the swine kidney. 2. The enzyme has been purified 110-fold by precipitation with ammonium sulphate, heat treatment and chromatography on Sephadex G-100. 3. The enzyme is heat-stable, but is rapidly inactivated below pH7. It requires Mg(2+) or Mn(2+) for activity. The Michaelis constant for leucine amide with Mg(2+)-activated enzyme is 5.0x10(-3)m. 4. Muscle leucine aminopeptidase is very similar to the kidney enzyme.
D000818:Animals; D011232:Chemical Precipitation; D002845:Chromatography; D004586:Electrophoresis; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007931:Leucyl Aminopeptidase / Q000032:analysis*; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology*; D013552:Swine
D008345:Manganese; D007931:Leucyl Aminopeptidase; D008274:Magnesium