Colicin S8 export: extracellular and cytoplasmic colicin are different
Int. microbiol
; 6(4): 263-267, dic. 2003. ilus, tab, tab, ilus
Article
in En
| IBECS
| ID: ibc-98746
Responsible library:
ES1.1
Localization: BNCS
ABSTRACT
The properties of colicin S8 are different for the cytoplasmic, periplasmic and extracellular protein. Interactions with its specific receptors reflect this. Active cell extracts separate into a non-anionic along with an anionic fraction by DEAE-Sephacell chromatography. Previously, we have purified cell-associated colicin S8 as an aggregation of highly related polypeptides; cytoplasmic colicin S8 seems to be post-translationally processed into an aggregation of polypeptides of molecular mass ranging from 45,000 Da to 60,000 Da. We suggest that a conformational change to colicin S8 may occur related to the export process (AU)
RESUMEN
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Collection:
06-national
/
ES
Database:
IBECS
Main subject:
Colicins
/
Escherichia coli
Language:
En
Journal:
Int. microbiol
Year:
2003
Document type:
Article