High-affinity binding of fungal beta-glucan fragments to soybean (Glycine max L.) microsomal fractions and protoplasts.
Identifieur interne : 002D65 ( Main/Exploration ); précédent : 002D64; suivant : 002D66High-affinity binding of fungal beta-glucan fragments to soybean (Glycine max L.) microsomal fractions and protoplasts.
Auteurs : E G Cosio [Allemagne] ; H. Pöpperl ; W E Schmidt ; J. EbelSource :
- European journal of biochemistry [ 0014-2956 ] ; 1988.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Glucanes, Membranes intracellulaires, Microsomes, Plantes, Protoplastes.
- Cinétique, Phytophthora, Radio-isotopes de l'iode, Soja.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glucans.
- metabolism : Intracellular Membranes, Microsomes, Plants, Protoplasts.
- chemical : Iodine Radioisotopes, Kinetics, Phytophthora, Soybeans.
Abstract
We have recently reported the existence of binding sites in soybean membranes for a beta-glucan fraction derived from the fungal pathogen Phytophthora megasperma f. sp. glycinea, which may play a role in the elicitor-mediated phytoalexin response of this plant [Schmidt, W. E. & Ebel, J. (1987) Proc. Natl Acad. Sci. USA 84, 4117-4121]. The specificity of beta-glucan binding to soybean membranes has now been investigated using a variety of competing polyglucans and oligoglucans of fungal origin. P. megasperma beta-glucan binding showed high apparent affinity for branched glucans with degrees of polymerization greater than 12. Binding affinity showed good correlation with elicitor activity as measured in a soybean cotyledon bioassay. Modification of the glucans at the reducing end with phenylalkylamine reagents had no effect on binding affinity. This characteristic was used to synthesize an oligoglucosyl tyramine derivative suitable for radioiodination. The 125I-glucan (15-30 Ci/mmol) provided higher sensitivity and lower detection limits for the binding assays while behaving in a manner identical to the [3H]glucan used previously. More accurate determinations of the Kd value for glucan binding indicated a higher affinity than previously shown (37 nM versus 200 nM). The 125I-glucan was used to provide the first reported evidence of specific binding of a fungal beta-glucan fraction in vivo to soybean protoplasts. The binding affinity to protoplasts proved identical to that found in microsomal fractions.
DOI: 10.1111/j.1432-1033.1988.tb14198.x
PubMed: 3402458
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Pöpperl</name></author><author><name sortKey="Schmidt, W E" sort="Schmidt, W E" uniqKey="Schmidt W" first="W E" last="Schmidt">W E Schmidt</name></author><author><name sortKey="Ebel, J" sort="Ebel, J" uniqKey="Ebel J" first="J" last="Ebel">J. 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Pöpperl</name></author><author><name sortKey="Schmidt, W E" sort="Schmidt, W E" uniqKey="Schmidt W" first="W E" last="Schmidt">W E Schmidt</name></author><author><name sortKey="Ebel, J" sort="Ebel, J" uniqKey="Ebel J" first="J" last="Ebel">J. Ebel</name></author></analytic><series><title level="j">European journal of biochemistry</title><idno type="ISSN">0014-2956</idno><imprint><date when="1988" type="published">1988</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Glucans (metabolism)</term><term>Intracellular Membranes (metabolism)</term><term>Iodine Radioisotopes (MeSH)</term><term>Kinetics (MeSH)</term><term>Microsomes (metabolism)</term><term>Phytophthora (MeSH)</term><term>Plants (metabolism)</term><term>Protoplasts (metabolism)</term><term>Soybeans (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Glucanes (métabolisme)</term><term>Membranes intracellulaires (métabolisme)</term><term>Microsomes (métabolisme)</term><term>Phytophthora (MeSH)</term><term>Plantes (métabolisme)</term><term>Protoplastes (métabolisme)</term><term>Radio-isotopes de l'iode (MeSH)</term><term>Soja (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucans</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Intracellular Membranes</term><term>Microsomes</term><term>Plants</term><term>Protoplasts</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glucanes</term><term>Membranes intracellulaires</term><term>Microsomes</term><term>Plantes</term><term>Protoplastes</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Iodine Radioisotopes</term><term>Kinetics</term><term>Phytophthora</term><term>Soybeans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Phytophthora</term><term>Radio-isotopes de l'iode</term><term>Soja</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have recently reported the existence of binding sites in soybean membranes for a beta-glucan fraction derived from the fungal pathogen Phytophthora megasperma f. sp. glycinea, which may play a role in the elicitor-mediated phytoalexin response of this plant [Schmidt, W. E. & Ebel, J. (1987) Proc. Natl Acad. Sci. USA 84, 4117-4121]. The specificity of beta-glucan binding to soybean membranes has now been investigated using a variety of competing polyglucans and oligoglucans of fungal origin. P. megasperma beta-glucan binding showed high apparent affinity for branched glucans with degrees of polymerization greater than 12. Binding affinity showed good correlation with elicitor activity as measured in a soybean cotyledon bioassay. Modification of the glucans at the reducing end with phenylalkylamine reagents had no effect on binding affinity. This characteristic was used to synthesize an oligoglucosyl tyramine derivative suitable for radioiodination. The 125I-glucan (15-30 Ci/mmol) provided higher sensitivity and lower detection limits for the binding assays while behaving in a manner identical to the [3H]glucan used previously. More accurate determinations of the Kd value for glucan binding indicated a higher affinity than previously shown (37 nM versus 200 nM). The 125I-glucan was used to provide the first reported evidence of specific binding of a fungal beta-glucan fraction in vivo to soybean protoplasts. The binding affinity to protoplasts proved identical to that found in microsomal fractions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3402458</PMID><DateCompleted><Year>1988</Year><Month>09</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-2956</ISSN><JournalIssue CitedMedium="Print"><Volume>175</Volume><Issue>2</Issue><PubDate><Year>1988</Year><Month>Aug</Month><Day>01</Day></PubDate></JournalIssue><Title>European journal of biochemistry</Title><ISOAbbreviation>Eur J Biochem</ISOAbbreviation></Journal><ArticleTitle>High-affinity binding of fungal beta-glucan fragments to soybean (Glycine max L.) microsomal fractions and protoplasts.</ArticleTitle><Pagination><MedlinePgn>309-15</MedlinePgn></Pagination><Abstract><AbstractText>We have recently reported the existence of binding sites in soybean membranes for a beta-glucan fraction derived from the fungal pathogen Phytophthora megasperma f. sp. glycinea, which may play a role in the elicitor-mediated phytoalexin response of this plant [Schmidt, W. E. & Ebel, J. (1987) Proc. Natl Acad. Sci. USA 84, 4117-4121]. The specificity of beta-glucan binding to soybean membranes has now been investigated using a variety of competing polyglucans and oligoglucans of fungal origin. P. megasperma beta-glucan binding showed high apparent affinity for branched glucans with degrees of polymerization greater than 12. Binding affinity showed good correlation with elicitor activity as measured in a soybean cotyledon bioassay. Modification of the glucans at the reducing end with phenylalkylamine reagents had no effect on binding affinity. This characteristic was used to synthesize an oligoglucosyl tyramine derivative suitable for radioiodination. The 125I-glucan (15-30 Ci/mmol) provided higher sensitivity and lower detection limits for the binding assays while behaving in a manner identical to the [3H]glucan used previously. More accurate determinations of the Kd value for glucan binding indicated a higher affinity than previously shown (37 nM versus 200 nM). The 125I-glucan was used to provide the first reported evidence of specific binding of a fungal beta-glucan fraction in vivo to soybean protoplasts. The binding affinity to protoplasts proved identical to that found in microsomal fractions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cosio</LastName><ForeName>E G</ForeName><Initials>EG</Initials><AffiliationInfo><Affiliation>Institut für Biologie II der Universität, Lehrstuhl für Biochemie der Pflanzen, Freiburg, Federal Republic of Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pöpperl</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Schmidt</LastName><ForeName>W E</ForeName><Initials>WE</Initials></Author><Author ValidYN="Y"><LastName>Ebel</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Eur J Biochem</MedlineTA><NlmUniqueID>0107600</NlmUniqueID><ISSNLinking>0014-2956</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005936">Glucans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007457">Iodine Radioisotopes</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D005936" MajorTopicYN="N">Glucans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007425" MajorTopicYN="N">Intracellular Membranes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007457" MajorTopicYN="N">Iodine Radioisotopes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008861" MajorTopicYN="N">Microsomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011523" MajorTopicYN="N">Protoplasts</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013025" MajorTopicYN="N">Soybeans</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1988</Year><Month>8</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1988</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1988</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3402458</ArticleId><ArticleId IdType="doi">10.1111/j.1432-1033.1988.tb14198.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bade-Wurtemberg</li><li>District de Fribourg-en-Brisgau</li></region><settlement><li>Fribourg-en-Brisgau</li></settlement></list><tree><noCountry><name sortKey="Ebel, J" sort="Ebel, J" uniqKey="Ebel J" first="J" last="Ebel">J. Ebel</name><name sortKey="Popperl, H" sort="Popperl, H" uniqKey="Popperl H" first="H" last="Pöpperl">H. Pöpperl</name><name sortKey="Schmidt, W E" sort="Schmidt, W E" uniqKey="Schmidt W" first="W E" last="Schmidt">W E Schmidt</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Cosio, E G" sort="Cosio, E G" uniqKey="Cosio E" first="E G" last="Cosio">E G Cosio</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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