Expression of sporophytic storage proteins in the corm of the quillwort (Isoetes echinospora Dur.)
Parenchyma cells from the corm tissue of the aquatic lycopod Isoetes echinospora Dur. were shown by electron microscopy to be packed with amyloplasts, lipid bodies, and protein bodies. The protein bodies are morphologically similar to those identified in seeds and certain vegetative tissues of highe...
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| Veröffentlicht in: | Plant physiology (Bethesda) 1994-12, Vol.106 (4), p.1395-1402 |
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| creator | DeCamp, J.D. (Harvard University, Cambridge, MA.) Stetler, D.A DeMaggio, A.E |
| description | Parenchyma cells from the corm tissue of the aquatic lycopod Isoetes echinospora Dur. were shown by electron microscopy to be packed with amyloplasts, lipid bodies, and protein bodies. The protein bodies are morphologically similar to those identified in seeds and certain vegetative tissues of higher plants. Globoid-containing protein bodies (1-10 micrometers) isolated in a sucrose gradient possessed a buoyant density of 1.28 g/mL and contained globulin (salt-soluble) proteins. Sucrose gradient centrifugation of crude globulins revealed only two components with mean sedimentation coefficients of approximately 2S and 11S. The 2S component, designated VSP-IsA, was composed of a 15.7-kD polypeptide. The 11S component, designated VSP-IsB, had a molecular mass of 215 kD as estimated by gel filtration and was composed of 39- to 42-kD polypeptides. Two-dimensional gel electrophoresis showed constituent polypeptides distinguished by differences in net charge and molecular mass. Affinity-purified antibodies against VSP-IsA and VSP-IsB prepared and used as probes on immunoblots crossreact only with their specific antigens, suggesting that the proteins are not immunologically related. Indirect immunolocalization studies confirmed that VSP-IsB is deposited in protein bodies. These globulin proteins, like those from some seeds, form the principal storage reserves of the corm tissue |
| doi_str_mv | 10.1104/pp.106.4.1395 |
| format | Article |
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(Harvard University, Cambridge, MA.) ; Stetler, D.A ; DeMaggio, A.E</creator><creatorcontrib>DeCamp, J.D. (Harvard University, Cambridge, MA.) ; Stetler, D.A ; DeMaggio, A.E</creatorcontrib><description>Parenchyma cells from the corm tissue of the aquatic lycopod Isoetes echinospora Dur. were shown by electron microscopy to be packed with amyloplasts, lipid bodies, and protein bodies. The protein bodies are morphologically similar to those identified in seeds and certain vegetative tissues of higher plants. Globoid-containing protein bodies (1-10 micrometers) isolated in a sucrose gradient possessed a buoyant density of 1.28 g/mL and contained globulin (salt-soluble) proteins. Sucrose gradient centrifugation of crude globulins revealed only two components with mean sedimentation coefficients of approximately 2S and 11S. The 2S component, designated VSP-IsA, was composed of a 15.7-kD polypeptide. The 11S component, designated VSP-IsB, had a molecular mass of 215 kD as estimated by gel filtration and was composed of 39- to 42-kD polypeptides. Two-dimensional gel electrophoresis showed constituent polypeptides distinguished by differences in net charge and molecular mass. Affinity-purified antibodies against VSP-IsA and VSP-IsB prepared and used as probes on immunoblots crossreact only with their specific antigens, suggesting that the proteins are not immunologically related. Indirect immunolocalization studies confirmed that VSP-IsB is deposited in protein bodies. These globulin proteins, like those from some seeds, form the principal storage reserves of the corm tissue</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.106.4.1395</identifier><identifier>PMID: 12232417</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>ANATOMIA DE LA PLANTA ; ANATOMIE VEGETALE ; Antibodies ; Bark ; Biological and medical sciences ; Cell biochemistry ; Cell physiology ; Centrifugation ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; CORMO ; Corms ; CORMUS ; Development and Growth Regulation ; ESTRUCTURA CELULAR ; Fundamental and applied biological sciences. Psychology ; Gels ; GLOBULINAS ; GLOBULINE ; Globulins ; IMMUNOLOGIE ; INMUNOLOGIA ; NEW HAMPSHIRE ; Nitrogen ; Parenchyma ; PARENCHYME ; PARENQUIMA ; Plant physiology and development ; PLANTAS ACUATICAS ; PLANTE AQUATIQUE ; Plants ; PROTEINAS ; PROTEINE ; PTERIDOPHYTA ; PURIFICACION ; PURIFICATION ; Storage proteins ; STRUCTURE CELLULAIRE ; VERMONT</subject><ispartof>Plant physiology (Bethesda), 1994-12, Vol.106 (4), p.1395-1402</ispartof><rights>Copyright 1994 American Society of Plant Physiologists</rights><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4276213$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4276213$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3372671$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12232417$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>DeCamp, J.D. (Harvard University, Cambridge, MA.)</creatorcontrib><creatorcontrib>Stetler, D.A</creatorcontrib><creatorcontrib>DeMaggio, A.E</creatorcontrib><title>Expression of sporophytic storage proteins in the corm of the quillwort (Isoetes echinospora Dur.)</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Parenchyma cells from the corm tissue of the aquatic lycopod Isoetes echinospora Dur. were shown by electron microscopy to be packed with amyloplasts, lipid bodies, and protein bodies. The protein bodies are morphologically similar to those identified in seeds and certain vegetative tissues of higher plants. Globoid-containing protein bodies (1-10 micrometers) isolated in a sucrose gradient possessed a buoyant density of 1.28 g/mL and contained globulin (salt-soluble) proteins. Sucrose gradient centrifugation of crude globulins revealed only two components with mean sedimentation coefficients of approximately 2S and 11S. The 2S component, designated VSP-IsA, was composed of a 15.7-kD polypeptide. The 11S component, designated VSP-IsB, had a molecular mass of 215 kD as estimated by gel filtration and was composed of 39- to 42-kD polypeptides. Two-dimensional gel electrophoresis showed constituent polypeptides distinguished by differences in net charge and molecular mass. Affinity-purified antibodies against VSP-IsA and VSP-IsB prepared and used as probes on immunoblots crossreact only with their specific antigens, suggesting that the proteins are not immunologically related. Indirect immunolocalization studies confirmed that VSP-IsB is deposited in protein bodies. These globulin proteins, like those from some seeds, form the principal storage reserves of the corm tissue</description><subject>ANATOMIA DE LA PLANTA</subject><subject>ANATOMIE VEGETALE</subject><subject>Antibodies</subject><subject>Bark</subject><subject>Biological and medical sciences</subject><subject>Cell biochemistry</subject><subject>Cell physiology</subject><subject>Centrifugation</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>CORMO</subject><subject>Corms</subject><subject>CORMUS</subject><subject>Development and Growth Regulation</subject><subject>ESTRUCTURA CELULAR</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>GLOBULINAS</subject><subject>GLOBULINE</subject><subject>Globulins</subject><subject>IMMUNOLOGIE</subject><subject>INMUNOLOGIA</subject><subject>NEW HAMPSHIRE</subject><subject>Nitrogen</subject><subject>Parenchyma</subject><subject>PARENCHYME</subject><subject>PARENQUIMA</subject><subject>Plant physiology and development</subject><subject>PLANTAS ACUATICAS</subject><subject>PLANTE AQUATIQUE</subject><subject>Plants</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PTERIDOPHYTA</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Storage proteins</subject><subject>STRUCTURE CELLULAIRE</subject><subject>VERMONT</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNpVkb1vFDEQxS0EIkegpEEIuaAIxS0ef6ztggKFAJEiUUBqy-vz3jnaWzv2LpD_Hq_udEA1T3q_eTPSQ-glkAaA8PcpNUDahjfAtHiEViAYXVPB1WO0IqRqopQ-Q89KuSOEAAP-FJ0BpYxykCvUXf1O2ZcS4ohjj0uKOabdwxQcLlPMdutxynHyYSw4jHjaeexi3i_sou_nMAy_Yp7wxXWJfvIFe7cLY1yCLP405-bdc_Skt0PxL47zHN1-vvpx-XV98-3L9eXHm7XjvJ3WPQEiZA-SCe6JlJZ5K4Bb2XHt-k2rteusYo61VDEFyltNBGy6TvVSg_TsHH045Ka52_uN8-OU7WBSDnubH0y0wfzvjGFntvGnAaFbqer-xXE_x_vZl8nsQ3F-GOzo41wMKKFZ5aiu6PqAuhxLyb4_XQFillpMSlW2hpullsq_-fe1v_Sxhwq8PQK2ODv02Y4ulBPHmKSthIq9PmB3Szknm1PZUmDVfnWwexuN3eaacPtdC86IFOwP82qogA</recordid><startdate>19941201</startdate><enddate>19941201</enddate><creator>DeCamp, J.D. (Harvard University, Cambridge, MA.)</creator><creator>Stetler, D.A</creator><creator>DeMaggio, A.E</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19941201</creationdate><title>Expression of sporophytic storage proteins in the corm of the quillwort (Isoetes echinospora Dur.)</title><author>DeCamp, J.D. (Harvard University, Cambridge, MA.) ; Stetler, D.A ; DeMaggio, A.E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-f01057f17354e077a3ea514a7b49cfd699cba83c36283818ea9051dbb8f7917e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>ANATOMIA DE LA PLANTA</topic><topic>ANATOMIE VEGETALE</topic><topic>Antibodies</topic><topic>Bark</topic><topic>Biological and medical sciences</topic><topic>Cell biochemistry</topic><topic>Cell physiology</topic><topic>Centrifugation</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>CORMO</topic><topic>Corms</topic><topic>CORMUS</topic><topic>Development and Growth Regulation</topic><topic>ESTRUCTURA CELULAR</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>GLOBULINAS</topic><topic>GLOBULINE</topic><topic>Globulins</topic><topic>IMMUNOLOGIE</topic><topic>INMUNOLOGIA</topic><topic>NEW HAMPSHIRE</topic><topic>Nitrogen</topic><topic>Parenchyma</topic><topic>PARENCHYME</topic><topic>PARENQUIMA</topic><topic>Plant physiology and development</topic><topic>PLANTAS ACUATICAS</topic><topic>PLANTE AQUATIQUE</topic><topic>Plants</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PTERIDOPHYTA</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Storage proteins</topic><topic>STRUCTURE CELLULAIRE</topic><topic>VERMONT</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>DeCamp, J.D. (Harvard University, Cambridge, MA.)</creatorcontrib><creatorcontrib>Stetler, D.A</creatorcontrib><creatorcontrib>DeMaggio, A.E</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>DeCamp, J.D. (Harvard University, Cambridge, MA.)</au><au>Stetler, D.A</au><au>DeMaggio, A.E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of sporophytic storage proteins in the corm of the quillwort (Isoetes echinospora Dur.)</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1994-12-01</date><risdate>1994</risdate><volume>106</volume><issue>4</issue><spage>1395</spage><epage>1402</epage><pages>1395-1402</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>Parenchyma cells from the corm tissue of the aquatic lycopod Isoetes echinospora Dur. were shown by electron microscopy to be packed with amyloplasts, lipid bodies, and protein bodies. The protein bodies are morphologically similar to those identified in seeds and certain vegetative tissues of higher plants. Globoid-containing protein bodies (1-10 micrometers) isolated in a sucrose gradient possessed a buoyant density of 1.28 g/mL and contained globulin (salt-soluble) proteins. Sucrose gradient centrifugation of crude globulins revealed only two components with mean sedimentation coefficients of approximately 2S and 11S. The 2S component, designated VSP-IsA, was composed of a 15.7-kD polypeptide. The 11S component, designated VSP-IsB, had a molecular mass of 215 kD as estimated by gel filtration and was composed of 39- to 42-kD polypeptides. Two-dimensional gel electrophoresis showed constituent polypeptides distinguished by differences in net charge and molecular mass. Affinity-purified antibodies against VSP-IsA and VSP-IsB prepared and used as probes on immunoblots crossreact only with their specific antigens, suggesting that the proteins are not immunologically related. Indirect immunolocalization studies confirmed that VSP-IsB is deposited in protein bodies. These globulin proteins, like those from some seeds, form the principal storage reserves of the corm tissue</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>12232417</pmid><doi>10.1104/pp.106.4.1395</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Plant physiology (Bethesda), 1994-12, Vol.106 (4), p.1395-1402 |
| issn | 0032-0889 1532-2548 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_159678 |
| source | JSTOR Archive Collection A-Z Listing; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | ANATOMIA DE LA PLANTA ANATOMIE VEGETALE Antibodies Bark Biological and medical sciences Cell biochemistry Cell physiology Centrifugation COMPOSICION QUIMICA COMPOSITION CHIMIQUE CORMO Corms CORMUS Development and Growth Regulation ESTRUCTURA CELULAR Fundamental and applied biological sciences. Psychology Gels GLOBULINAS GLOBULINE Globulins IMMUNOLOGIE INMUNOLOGIA NEW HAMPSHIRE Nitrogen Parenchyma PARENCHYME PARENQUIMA Plant physiology and development PLANTAS ACUATICAS PLANTE AQUATIQUE Plants PROTEINAS PROTEINE PTERIDOPHYTA PURIFICACION PURIFICATION Storage proteins STRUCTURE CELLULAIRE VERMONT |
| title | Expression of sporophytic storage proteins in the corm of the quillwort (Isoetes echinospora Dur.) |
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