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.
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