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Purification and enzymatic properties of an l -leucine aminopeptidase from swine liver

Biochimica et Biophysica Acta (BBA) - Enzymology, ISSN: 0005-2744, Vol: 660, Issue: 2, Page: 262-270
1981
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An l -leucine aminopeptidase (α-aminoacyl-peptide hydrolase (cytosol), EC 3.4.11.1), having a specificity toward the substrate l -leucine amide, but not toward l -leucyl β-naphthylamide or l -leucyl p -nitroanilide, has been purified 332-fold from swine liver, with a yield of 8.6%. This is the first purification of this enzyme from hepatic tissue. The purified enzyme submitted to analytical electrophoresis on cellulose acetate strips or in polyacrylamide gel showed a single band after staining with Ponceau S Red dye or Amido black, respectively. Purified swine liver l -leucine aminopeptidase, a cytosol enzyme, exhibited a molecular weight of 268 000 ± 50 000 by gel filtration. It hydrolyzed l -leucine amide substrate and l -leucyl peptides. It was activated by Mg 2+ and Mn 2+ and inhibited by Co 2+ and Zn 2+. The optimum pH was 10. It was rather sensitive to heat elevation. Swine liver l -leucine aminopeptidase was inhibited by EDTA, citric acid, isocaproic acid, dodecylamine, aliphatic alcohols and p -chloromercuribenzoate but unaffected by monoiodoacetic acid and diisopropyl fluorophosphate.

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