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Acid and Alkaline Phosphatases of Vibrio parahaemolyticus
Author(s) -
Sakaguchi Osamu,
Yokota Katushi,
Koshi Tomoyuki
Publication year - 1972
Publication title -
japanese journal of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0021-5139
DOI - 10.1111/j.1348-0421.1972.tb00670.x
Subject(s) - vibrio parahaemolyticus , alkaline phosphatase , phosphatase , chemistry , biochemistry , phosphate , acid phosphatase , ethylenediaminetetraacetic acid , chromatography , enzyme , biology , bacteria , inorganic chemistry , chelation , genetics
Characteristics of phosphatases of Vibrio parahaemolyticus A55 K + 105 were investigated. Phosphatases were extracted from intact cells in a 3% NaCl solution by gentle treatment on a reciprocal shaker for 15 min. The pH dependence of phosphatase of the extracts showed two optima; one optimum was found at pH 5.1–5.7, the other at pH 10.5–11.1, and the results were identical with that of resting cells. The activities of both acid and alkaline phosphatases were maximum in the presence of 0.1 m salt (KCl or NaCl). The production of alkaline phosphatase of resting cells in the induction medium containing p ‐nitrophenylphosphate was largely suppressed by the addition of 0.5% phosphate into the medium. The alkaline phosphatase of the extracts was stimulated about 2.5‐fold by the addition of 10 −3 m Mg ++ or Zn ++ , whereas it was inhibited completely by 10 −3 m ethylenediaminetetraacetic acid. On the other hand, Co ++ activated acid phosphatase to 98‐fold. Both acid and alkaline phosphatases were found in the culture filtrated after cultivation of the organism in a 3% NaCl‐nutrient broth medium for 16 hr.