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Biosci Biotechnol Biochem ; 66(6): 1366-9, 2002 Jun.
Article in English | MEDLINE | ID: mdl-12162559

ABSTRACT

The gene (empI) encoding an extracellular metal protease was isolated from a Pseudoalteromonas sp. strain A28 DNA library. The recombinant EmpI protein was expressed in E. coli and purified. Paper-disk assays showed that the purified protease had potent algicidal activity. A skim milk-polyacrylamide gel electrophoresis protease assay showed that the 38-kDa band of protease activity, which co-migrated with purified EmpI and was sensitive to 1,10-phenathroline, was detected in the extracellular supernatant of A28.


Subject(s)
Endopeptidases/genetics , Endopeptidases/metabolism , Metals/metabolism , Pseudoalteromonas/enzymology , Pseudoalteromonas/genetics , Cloning, Molecular , Electrophoresis, Polyacrylamide Gel , Endopeptidases/chemistry , Endopeptidases/isolation & purification , Molecular Weight , Restriction Mapping
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