A Novel Protein with Alkaline Phosphatase and Protease Inhibitor Activities in Streptomyces hiroshimensis.

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  • Nitta Masayuki
    Second Department of Hygienic Chemistry, Tohoku Pharmaceutical University
  • Goto Mariko
    Second Department of Hygienic Chemistry, Tohoku Pharmaceutical University
  • Shibuya Naomi
    Second Department of Hygienic Chemistry, Tohoku Pharmaceutical University
  • Okawa Yoshio
    Second Department of Hygienic Chemistry, Tohoku Pharmaceutical University

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  • Novel Protein with Alkaline Phosphatase and Protease Inhibitor Activities in Streptomyces hiroshimensis

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Abstract

A novel alkaline phosphatase (S-ALP) was found in the culture filtrate of Streptomyces hiroshimensis IFO 12785. Purification was achieved on Sephadex G-75 column, palmitoylated gauze column, and Superdex 75 HR column chromatographies. The molecular weight of S-ALP was estimated to be 14200 by sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE). The isoelectric point is 9.2. S-ALP had maximum enzyme activity at pH 9.5. S-ALP efficiently catalyzed both p-nitrophenyl phosphate and p-nitrophenyl phosphorylcholine substrates, particularly the latter. The N-terminal amino acid sequence (25 residues) of S-ALP was 60 to 72% identical to that of Streptomyces subtilisin inhibitor-like proteins. S-ALP exhibited trypsin inhibition in addition to a strong inhibition of subtilisin.

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