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- W2155804181 abstract "Proline iminopeptidase (EC 3.4.13.8-9) is an aminopeptidase which can release specifically an amino-terminal proline residue from short peptides. We purified and characterized an iminopeptidase from cotyledons of peanuts by saline precipitation, ionic exchange in DEAE–Sepharose at pH 6.2 and 7.4, and preparative electrophoresis. The purified enzyme had a molecular weight of about 220 kDa by gel filtration. By sodium dodecyl sulfate–polyacrylamide gel electrophoresis, only a band of molecular weight of about 55 kDa was obtained, suggesting the oligomeric nature of iminopeptidase. An antiserum raised against the whole enzyme recognized a coincident single band on nitrocellulose-blots following denaturating gel electrophoresis of peanut cotyledons protein, supporting the hypothesis that this polypeptide is a subunit of enzyme. Optimal activity of the purified enzyme with l-proline–p-nitroanilide was observed at pH 8. The enzyme was inhibited by p-hydroxymercuribenzoate and N-ethylmaleimide, but was also inhibited by Phenylmethanesulphonyl fluoride and diisopropyl fluorphosphate. These results suggest that the enzyme cysteine and serine residues may participate in the enzyme activity. Twelve aminoacyl-β-naphtylamides were tested as substrates. Iminopeptidase hydrolyzed preferentially pro-β-naphtylamide but shows significant activity also against the derivatives of leu, met and ala. Short peptides with amino-terminal proline were hydrolyzed by the enzyme with variable intensity, but significant hydrolysis of salmine, a protein with the same N-terminus, was not detected." @default.
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- W2155804181 date "2004-05-01" @default.
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- W2155804181 title "Purification and properties of iminopeptidase from peanut seeds" @default.
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- W2155804181 doi "https://doi.org/10.1016/j.plantsci.2003.12.009" @default.
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