Purification and properties of haloacetate halidohydrolase specified by plasmid from Moraxella sp. strain B.

• KAWASAKI Haruhiko

  Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture

• TONE Noriko

  Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture

• TONOMURA Kenzo

  Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture

Abstract

Haloacetate halidohydrolase II specified by a plasmid pUO1 was purified from haloacetateassimilating Moraxella sp. B. The purification procedures included protamine treatment, Ammonium sulfate fractionation, and column chromatographies with DEAE-cellulose, hydroxyapatite and Bio-gel P-150, resulting in a 200-fold purification. The purified enzyme was homogeneous by criteria of ultracentrifugation and disc electrophoresis.<br> The molecular weight estimated by Sephadex G-100 gel filtration was 43, 000, and it was 26, 000 by SDS-polyacrylamide gel electrophoresis. The sedimentation coefficient s⁰_{20, w} was 4.1 S, and the isoelectric point was pH5.2. The amino acid composition was also estimated.<br> The enzyme catalyzed the dehalogenation of monochloro-, monobromo-and monoiodoacetate, but not monofluoroacetate. 2, 2-Dichloroacetate and 2-chloropropionate were slightly dehalogenated, but trichloroacetate and 3-chloropropionate were not. The enzymewas very sensitive to inhibition with thiol reagents.

Journal

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 45 (1), 35-42, 1981

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

Details

• CRID: 1390001206465117568
• NII Article ID: 130000028808
• DOI: 10.1271/bbb1961.45.35
• COI: 1:CAS:528:DyaL3MXpvVGntg%3D%3D
• ISSN: 18811280
• ISSN: 00021369
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed