Source:http://linkedlifedata.com/resource/pubmed/id/16661873
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2010-6-29
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| pubmed:abstractText |
The ability of beta-glucosylase I, a soybean cell wall beta-glucosyl hydrolase, to degrade elicitors of phytoalexin accumulation was studied. Extensive beta-glucosylase I treatment of the glucan elicitor isolated from the mycelial walls of Phytophthora megasperma var. sojae results in hydrolysis of 77% of the glucosidic bonds of the elicitor and destruction of 94% of its activity. Soybean cell walls contain some additional factor, probably one or more additional enzymes, which can assist beta-glucosylase I in hydrolyzing the glucan elicitor. This was demonstrated by the more rapid hydrolysis of the glucan elicitor by a mixture of soybean cell wall enzymes (containing beta-glucosylase I). In a single treatment, the mixture of cell wall enzymes hydrolyzed 91% of the glucosidic bonds and destroyed 85% of the activity of the elicitor. The enzymes from soybean cell walls will also hydrolyze elicitor-active oligoglucosides prepared from the mycelial walls of Phytophthora megasperma var. sojae. The active oligoglucosides are more susceptible than the glucan elicitor to hydrolysis by these enzymes. The mixture of cell wall enzymes or beta-glucosylase I, by itself, hydrolyzes more than 96% of the glucosidic bonds and destroys more than 99% of the activity of the oligoglucoside elicitor. Two possible advantages for the existence of these enzymes in the walls of soybean cells are discussed.
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| pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-16657372,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-16659565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-16659566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-16660529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-16661872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-17735052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-17793733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-193853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-359568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-4368906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-677526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661873-965389
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0032-0889
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
68
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
221-8
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| pubmed:dateRevised |
2010-9-15
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| pubmed:year |
1981
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| pubmed:articleTitle |
Host-Pathogen Interactions : XVII. HYDROLYSIS OF BIOLOGICALLY ACTIVE FUNGAL GLUCANS BY ENZYMES ISOLATED FROM SOYBEAN CELLS.
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| pubmed:affiliation |
Department of Chemistry, University of Colorado, Boulder, Colorado 80309.
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| pubmed:publicationType |
Journal Article
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