Potassium Chloride → Deacetoxycephalosporin C

Participants

Reaction Steps

The fractions containing 80% of the enzyme activity from the major peak were pooled. The pooled fractions were supplemented with 0.1 mM penicillin N and were loaded onto a second Mono Q column (0.5×5 cm) which had been equilibrated with the glycerol-free buffer, pH 7.0, (instead of pH 8.0 for UDG buffer), which was supplemented with 0.05 M KCl. The bound proteins were eluted with a linear gradient of KCl 0.05-0.2 M) in the equilibration buffer. The activity and protein elution patterns are shown in FIG. 4A. The three fractions with a synthase activity of at least 275 mU/ml were pooled.

Provenance & Evidence