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A New Type of Streptomycete Arylsulfatase with High Affinity to the Sulfuryl Moiety of the Substrate
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...
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Published in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1995-06, Vol.59 (6), p.1069-1075 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.59.1069 |