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- W2040426342 abstract "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." @default.
- W2040426342 created "2016-06-24" @default.
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- W2040426342 date "1978-01-01" @default.
- W2040426342 modified "2023-09-26" @default.
- W2040426342 title "Isolation of aminopeptidases fromHistoplasma capsulatum" @default.
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- W2040426342 doi "https://doi.org/10.1080/00362177885380101" @default.
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