Mikamycin B lactonase was purified from the cell extract of Streptomyces mitakaensis, an organism producing mikamycin B. The purification procedure included ammonium sulfate precipitation followed by chromatography on columns of calcium phosphate-cellulose, DEAE-cellulose and Sephadex. The final enzyme preparation was 1400 fold purified and found to be homogeneous when examined by polyacrylamide gel electrophoresis. The molecular weight was calculated as 29, 000 and Km value for mikamycin B was 1.43×10-5M. It catalysed the hydrolysis of the lactone linkage of mikamycin B and staphylomycin antibiotics.
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Kim et al. (1976) studied this question.