Abstract
A heterologous phosphotriesterase (parathion hydrolase) was previosly shown to be secreted by Streptomyces lividans. To investigate the mechanism of secretion, a system to label the protein and follow its expression and secretion was developed. The recombinant S. lividans was grown first in a defined medium containing [35S]methionine that permitted expression but not secretion. It was then transferred to tryptone/glucose medium with unlabeled methionine for the chase period, during which secretion was observed. The results indicate a relatively slow rate of secretion that is also dependent on the growth medium.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 493-497 |
| Number of pages | 5 |
| Journal | Applied Microbiology and Biotechnology |
| Volume | 43 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jul 1995 |
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