A novel protein with alkaline phosphatase and protease inhibitor activities in Streptomyces hiroshimensis

Biological & Pharmaceutical Bulletin
Masayuki NittaYoshio Okawa

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.

References

Jan 1, 1978·Microbiology and Immunology·Y Okawa, T Yamaguchi
Apr 24, 1989·FEBS Letters·Y Kourteva, R Boteva
Oct 1, 1985·Analytical Biochemistry·P K SmithD C Klenk
May 1, 1971·The Biochemical Journal·M K Majumdar, S K Majumdar
May 1, 1997·Journal of Molecular Evolution·S TaguchiH Momose

Citations

Sep 22, 2018·Journal of Basic Microbiology·Darina Blagovest Dimitrova-Stefanova, Blagovesta Todorova Gocheva

Related Concepts

Alkaline Phosphatase
Bacterial Proteins
Catalysis
Molecular Sieve Chromatography
SDS-PAGE
Isoelectric Point
Protease Inhibitors
Streptomyces
Substrate Specificity
Trypsin Inhibitors

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