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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1995-5-10
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pubmed:abstractText |
In previous studies (Malissard et al., FEMS Microbiol. Lett. (1993) 110, 101-106), the alginate lyase AlxM of the marine bacterium ATCC 433367 was produced in Escherichia coli TC4/pAL-A3 with a yield of 50 micrograms per litre of culture. The polypeptide chain was cleaved between two cysteine residues, C169 and C183, themselves linked by a disulphide bridge. AlxM has now been overproduced in E. coli BL21(DE3)/pAL-Sur/pLysS. Under conditions in which formation of inclusion bodies can be avoided, the enzyme is synthesized as a catalytically active, water-soluble, unnicked polypeptide with a yield of 32 mg per litre of culture. It has been purified to protein homogeneity using a one-step procedure. The nicked AlxMA and unnicked AlxMB alginate lyases have identical alginate-degrading activities at high salt concentrations.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0378-1097
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
126
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
105-11
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7705601-Amino Acid Sequence,
pubmed-meshheading:7705601-Base Sequence,
pubmed-meshheading:7705601-Cloning, Molecular,
pubmed-meshheading:7705601-Escherichia coli,
pubmed-meshheading:7705601-Molecular Sequence Data,
pubmed-meshheading:7705601-Plasmids,
pubmed-meshheading:7705601-Polysaccharide-Lyases
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pubmed:year |
1995
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pubmed:articleTitle |
Overproduction and properties of the mannuronate alginate lyase AlxMB.
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pubmed:affiliation |
Laboratoire de Biochimie Microbienne, Université Claude Bernard, Villeurbanne, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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