The 32-Kilodalton Vegetative Storage Protein of Salix microstachya Turz : Characterization and Immunolocalization.
Identifieur interne : 004C34 ( Main/Exploration ); précédent : 004C33; suivant : 004C35The 32-Kilodalton Vegetative Storage Protein of Salix microstachya Turz : Characterization and Immunolocalization.
Auteurs : S. Wetzel [Canada] ; J S GreenwoodSource :
- Plant physiology [ 0032-0889 ] ; 1991.
Abstract
A 32-kilodalton vegetative storage protein, found in Salix microstachya Turz. bark during the overwintering period, was purified and characterized using several polyacrylamide gel electrophoretic procedures. Solubility characteristics and amino acid analyses were also performed. The protein is water soluble, is glycosylated, has no disulfide-bonded subunits, but is composed of a family of isoelectric isomers. The majority of these isomers are basic. Characteristic of storage proteins, the protein is rich in glutamine/glutamate and asparagine/aspartate (28%), the basic nature of the isomers indicating that most of these amino acid residues are in the amide form. The protein was purified using preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis and antibodies raised in chickens. Immunoblot analysis suggested an annual cyclic nature of the accumulation and mobilization of this vegetative storage protein. Immunologically, it is related to a similar molecular weight protein found in the bark of Populus deltoides Marsh. but not to any overwintering storage proteins of the other hardwoods tested. Indirect immunolocalization revealed that the protein was sequestered in protein-storage vacuoles in parenchymatous cells of the inner bark tissues of Salix during the winter months.
DOI: 10.1104/pp.97.2.771
PubMed: 16668465
PubMed Central: PMC1081073
Affiliations:
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Wetzel</name><affiliation wicri:level="1"><nlm:affiliation>Department of Botany, University of Guelph, Guelph, Ontario, Canada N1G 2W1.</nlm:affiliation><country>Canada</country><wicri:regionArea>Department of Botany, University of Guelph, Guelph, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author><author><name sortKey="Greenwood, J S" sort="Greenwood, J S" uniqKey="Greenwood J" first="J S" last="Greenwood">J S Greenwood</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:16668465</idno><idno type="pmid">16668465</idno><idno type="pmc">PMC1081073</idno><idno type="doi">10.1104/pp.97.2.771</idno><idno type="wicri:Area/Main/Corpus">004C40</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004C40</idno><idno type="wicri:Area/Main/Curation">004C40</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004C40</idno><idno type="wicri:Area/Main/Exploration">004C40</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The 32-Kilodalton Vegetative Storage Protein of Salix microstachya Turz : Characterization and Immunolocalization.</title><author><name sortKey="Wetzel, S" sort="Wetzel, S" uniqKey="Wetzel S" first="S" last="Wetzel">S. Wetzel</name><affiliation wicri:level="1"><nlm:affiliation>Department of Botany, University of Guelph, Guelph, Ontario, Canada N1G 2W1.</nlm:affiliation><country>Canada</country><wicri:regionArea>Department of Botany, University of Guelph, Guelph, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author><author><name sortKey="Greenwood, J S" sort="Greenwood, J S" uniqKey="Greenwood J" first="J S" last="Greenwood">J S Greenwood</name></author></analytic><series><title level="j">Plant physiology</title><idno type="ISSN">0032-0889</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A 32-kilodalton vegetative storage protein, found in Salix microstachya Turz. bark during the overwintering period, was purified and characterized using several polyacrylamide gel electrophoretic procedures. Solubility characteristics and amino acid analyses were also performed. The protein is water soluble, is glycosylated, has no disulfide-bonded subunits, but is composed of a family of isoelectric isomers. The majority of these isomers are basic. Characteristic of storage proteins, the protein is rich in glutamine/glutamate and asparagine/aspartate (28%), the basic nature of the isomers indicating that most of these amino acid residues are in the amide form. The protein was purified using preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis and antibodies raised in chickens. Immunoblot analysis suggested an annual cyclic nature of the accumulation and mobilization of this vegetative storage protein. Immunologically, it is related to a similar molecular weight protein found in the bark of Populus deltoides Marsh. but not to any overwintering storage proteins of the other hardwoods tested. Indirect immunolocalization revealed that the protein was sequestered in protein-storage vacuoles in parenchymatous cells of the inner bark tissues of Salix during the winter months.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">16668465</PMID><DateCompleted><Year>2010</Year><Month>06</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>97</Volume><Issue>2</Issue><PubDate><Year>1991</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>The 32-Kilodalton Vegetative Storage Protein of Salix microstachya Turz : Characterization and Immunolocalization.</ArticleTitle><Pagination><MedlinePgn>771-7</MedlinePgn></Pagination><Abstract><AbstractText>A 32-kilodalton vegetative storage protein, found in Salix microstachya Turz. bark during the overwintering period, was purified and characterized using several polyacrylamide gel electrophoretic procedures. Solubility characteristics and amino acid analyses were also performed. The protein is water soluble, is glycosylated, has no disulfide-bonded subunits, but is composed of a family of isoelectric isomers. The majority of these isomers are basic. Characteristic of storage proteins, the protein is rich in glutamine/glutamate and asparagine/aspartate (28%), the basic nature of the isomers indicating that most of these amino acid residues are in the amide form. The protein was purified using preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis and antibodies raised in chickens. Immunoblot analysis suggested an annual cyclic nature of the accumulation and mobilization of this vegetative storage protein. Immunologically, it is related to a similar molecular weight protein found in the bark of Populus deltoides Marsh. but not to any overwintering storage proteins of the other hardwoods tested. Indirect immunolocalization revealed that the protein was sequestered in protein-storage vacuoles in parenchymatous cells of the inner bark tissues of Salix during the winter months.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wetzel</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Botany, University of Guelph, Guelph, Ontario, Canada N1G 2W1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Greenwood</LastName><ForeName>J S</ForeName><Initials>JS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>10</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>10</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>10</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16668465</ArticleId><ArticleId IdType="pmc">PMC1081073</ArticleId><ArticleId IdType="doi">10.1104/pp.97.2.771</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Nature. 1970 Aug 15;227(5259):680-5</Citation><ArticleIdList><ArticleId IdType="pubmed">5432063</ArticleId></ArticleIdList></Reference><Reference><Citation>Electrophoresis. 1988 Nov;9(11):751-63</Citation><ArticleIdList><ArticleId IdType="pubmed">3250878</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1989 Jan;89(1):309-15</Citation><ArticleIdList><ArticleId IdType="pubmed">16666532</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4</Citation><ArticleIdList><ArticleId IdType="pubmed">388439</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Cell Biol. 1985 Jul;38(1):87-93</Citation><ArticleIdList><ArticleId IdType="pubmed">4029177</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1969 Jul;30(1):148-52</Citation><ArticleIdList><ArticleId IdType="pubmed">4183001</ArticleId></ArticleIdList></Reference><Reference><Citation>J Agric Food Chem. 1981 May-Jun;29(3):497-501</Citation><ArticleIdList><ArticleId IdType="pubmed">7195912</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1977 Dec;12(4):1133-41</Citation><ArticleIdList><ArticleId IdType="pubmed">23215</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 1990 Jan;2(1):1-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12354941</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1988 Apr;86(4):1027-31</Citation><ArticleIdList><ArticleId IdType="pubmed">16666026</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1984 Jul 1;221(1):163-9</Citation><ArticleIdList><ArticleId IdType="pubmed">6466312</ArticleId></ArticleIdList></Reference><Reference><Citation>J Immunol Methods. 1981;46(1):63-8</Citation><ArticleIdList><ArticleId IdType="pubmed">6169771</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Greenwood, J S" sort="Greenwood, J S" uniqKey="Greenwood J" first="J S" last="Greenwood">J S Greenwood</name></noCountry><country name="Canada"><noRegion><name sortKey="Wetzel, S" sort="Wetzel, S" uniqKey="Wetzel S" first="S" last="Wetzel">S. 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