| 摘要 |
Echinocandin B deacylase, a cell-associated enzyme from Actinoplanes utahensis, is purified to near homogeneity in a process comprising hydrophobic interaction chromatography, cation-exchange chromatography and gel filtrations. The enzyme is a heterodimer containing 18-KD and 63-KD subunits and is a simple enzyme unaffected in activity by co-factors, metal chelators, or sulfhydryl reagents. The enzyme catalyzes the deacylation of the lipid acyl portion of lipid cyclicpeptide metabolites such as ECB and aculeacin. |
