Abstract
An aminopeptidase was highly purified from a cellular extract ofTreponema phagedenis (Reiter strain) by ammonium sulfate precipitation and successive chromatography on Sepharose 6B, DEAE-Sepharose CL-6B and CM-Sepharose CL-6B. The molecular weight of the enzyme was 74,500. The enzyme was stable in the pH region 5.0–7.0 and up to 50°C. The optimal pH, ionic strength, and temperature were pH 7.9–8.0,I 0.13, and 37°C, respectively. Co2+ was essential for the enzyme activity with an optimal concentration of 0.3 mM, and EDTA and such divalent cations as Hg2+, Cu2+, Zn2+, Pb2+, Sn2+, and Cd2+ were inhibitory against the Co2+-activated enzyme. The enzyme exhibited a preference for hydrophobic residues as well as Arg in the N-terminal position and cleaved in the order of Tyr > Trp > Phe > Leu > Arg > Ala ≫ His, Met, and Ser, but did not cleave the other amino acids including Pro, Glu, Asp, and Lys.
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Takahashi, T., Asari, K., Sato, N. et al. Purification and properties of an aminopeptidase fromTreponema phagedenis (Reiter strain). Current Microbiology 12, 283–287 (1985). https://doi.org/10.1007/BF01567979
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DOI: https://doi.org/10.1007/BF01567979