New Arylsulfatases from Streptomycetes (III). A New Type of Streptomycete Arylsulfatase with High Affinity to the Sulfuryl Moiety of the Substrate.

• Ueki Tomokazu

• Sawada Yosuke

• Fukagawa Yasuo

• Oki Toshikazu

Bibliographic Information

Other Title

• A New Type of Streptomycete Arylsulfatase with High Affinity to the Sulfuryl Moiety of the Substrate

Abstract

Streptomyces sp. T109-3 arylsulfatase (Es-2), which desulfated p-nitrophenyl sulfate as well as etoposide 4'-sulfate, was purified to protein homogeneity by sulfated cellulose affinity and DEAE-cellulose column chromatographies. Es-2 required calcium for enzyme activity and was severely inhibited by SH and chelating reagents. Comparative characterization showed that, although distinct in recognition of the binding moiety of substrate, Es-1 (Streptomyces griseorubiginosus S980-14 arylsulfatase) and Es-2 shared high desulfating activity on etoposide 4'-sulfate and many other common enzymological characteristics, which suggested they would be acceptable as the enzyme component of antitumor antibody-enzyme conjugates for target chemotherapy.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 59 (6), 1069-1075, 1995

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• Organic Chemistry
• Molecular Biology
• Applied Microbiology and Biotechnology
• General Medicine
• Biochemistry
• Analytical Chemistry
• Biotechnology

Details

• CRID: 1390282681452106240
• NII Article ID: 110002677626
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.59.1069
• ISSN: 13476947
• ISSN: 09168451
• PubMed: 7612993
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.59.1069
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• Abstract License Flag: Disallowed