Isolation of aminopeptidases from Histoplasma capsulatum.
Two aminopeptidases (arylamidases) were isolated and partially purified from Histoplasma capsulatum. The larger molecular weight enzyme was a proline iminopeptidase and hydrolyzed primarily a synthetic substrate, L-prolyl-beta-napthylamide. The other aminopeptidase was less substrate specific and hydrolyzed rapidly the following amino acid beta-napthylamides (beta NA): L-arginyl-beta NA greater than L-lysyl-beta NA greater than -L-4-methoxy-leucyl-beta NA greater than L-leucyl-beta NA greater than L-phenylalanyl-beta NA greater than L-alanyl-beta NA. The proline iminopeptidase was purified 1420 fold while the leucine aminopeptidase was purified 650 fold with good recovery.
D000626:Aminopeptidases / Q000302:isolation & purification*; D000645:Ammonium Sulfate; D002498:Centrifugation; D005591:Chemical Fractionation; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006658:Histoplasma / Q000201:enzymology*; D006868:Hydrolysis; D007931:Leucyl Aminopeptidase / Q000302:isolation & purification / Q000378:metabolism
D000626:Aminopeptidases; D007931:Leucyl Aminopeptidase; D000645:Ammonium Sulfate