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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1998-12-17
|
| pubmed:abstractText |
The major laminarinase activity (EC 3.2.1.39) from the gastropodean marine mollusc Haliotis tuberculata was purified to homogeneity by cation exchange chromatography and its action pattern was investigated by HPAEC-PAD analysis of the degradation of various laminarin samples. It consists of a 60 kDa protein capable of depolymerizing the unbranched portions of the beta-(1-->3), beta-(1-->6)-glucan, down to laminaritriose. The enzyme operates via a molecular mechanism retaining the anomeric configuration. As the purified protein does not cleave the beta-(1-->6) linkages, it can be used for the structural analysis of laminarins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0008-6215
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
310
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
283-9
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9821264-Amino Acid Sequence,
pubmed-meshheading:9821264-Animals,
pubmed-meshheading:9821264-Chromatography, Ion Exchange,
pubmed-meshheading:9821264-Glucan Endo-1,3-beta-D-Glucosidase,
pubmed-meshheading:9821264-Hydrolysis,
pubmed-meshheading:9821264-Molecular Sequence Data,
pubmed-meshheading:9821264-Mollusca,
pubmed-meshheading:9821264-Polysaccharide-Lyases,
pubmed-meshheading:9821264-Protein Conformation
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Purification and determination of the action pattern of Haliotis tuberculata laminarinase.
|
| pubmed:affiliation |
Centre d'Etudes d'Océanographie et de Biologie Marine (CEOBM-CNRS UPR 9042) B.P. 74, Roscof, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|