Purification and developmental analysis of the major anionic peroxidase from the seed coat of Glycine max
We show that the majority of peroxidase activity in soybean (Glycine max var Williams 82) seeds is localized to the seed coat. A single isozyme is responsible for this activity and has been purified to electrophoretic homogeneity by successive chromatography on DEAE Sepharose Fast Flow, concanavalin...
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Veröffentlicht in: | Plant physiology (Bethesda) 1991-05, Vol.96 (1), p.214-220 |
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description | We show that the majority of peroxidase activity in soybean (Glycine max var Williams 82) seeds is localized to the seed coat. A single isozyme is responsible for this activity and has been purified to electrophoretic homogeneity by successive chromatography on DEAE Sepharose Fast Flow, concanavalin A-Sepharose, and Sephadex G-75. The peroxidase exhibits a pl of 4.1, an apparent molecular mass of 37 kilodaltons, and has properties characteristic of a glycoprotein. The enzyme begins to accumulate approximately 21 days after anthesis and continues to do so throughout the maturation of the seed coat where it can represent at least 5% of the soluble protein in dry seed coats. Due to its localization in the seed, we propose that this isozyme may play a role in the hardening of the seed cost |
doi_str_mv | 10.1104/pp.96.1.214 |
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Due to its localization in the seed, we propose that this isozyme may play a role in the hardening of the seed cost</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.96.1.214</identifier><identifier>PMID: 16668154</identifier><language>eng</language><publisher>United States: American Society of Plant Physiologists</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ANION ; ANIONES ; Cell walls ; Cellulose nitrate ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; CONTENIDO PROTEICO ; DURCISSEMENT ; ENDURECIMIENTO ; Enzymes ; Gels ; GLYCINE MAX ; ISOENZIMAS ; ISOENZYME ; Lignin ; PEROXIDASAS ; peroxidase ; PEROXYDASE ; Plant tissues ; Plants ; Polymerization ; PROPIEDADES FISICO-QUIMICAS ; PROPRIETE PHYSICOCHIMIQUE ; PROTEINAS ; PROTEINE ; PURIFICACION ; PURIFICATION ; seeds ; SEMENCE ; SEMILLAS ; Soybeans ; TENEUR EN PROTEINES ; TESTA</subject><ispartof>Plant physiology (Bethesda), 1991-05, Vol.96 (1), p.214-220</ispartof><rights>Copyright 1991 American Society of Plant Physiologists</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c495t-eb13da10719a58f3d3b2f05142422790ef6691931fe8e94dd03781d6db11b5313</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4273579$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4273579$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16668154$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gillikin, J.W. (Bowling Green State University, Bowling Green, OH)</creatorcontrib><creatorcontrib>Graham, J.S</creatorcontrib><title>Purification and developmental analysis of the major anionic peroxidase from the seed coat of Glycine max</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>We show that the majority of peroxidase activity in soybean (Glycine max var Williams 82) seeds is localized to the seed coat. A single isozyme is responsible for this activity and has been purified to electrophoretic homogeneity by successive chromatography on DEAE Sepharose Fast Flow, concanavalin A-Sepharose, and Sephadex G-75. The peroxidase exhibits a pl of 4.1, an apparent molecular mass of 37 kilodaltons, and has properties characteristic of a glycoprotein. The enzyme begins to accumulate approximately 21 days after anthesis and continues to do so throughout the maturation of the seed coat where it can represent at least 5% of the soluble protein in dry seed coats. Due to its localization in the seed, we propose that this isozyme may play a role in the hardening of the seed cost</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>ANION</subject><subject>ANIONES</subject><subject>Cell walls</subject><subject>Cellulose nitrate</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>CONTENIDO PROTEICO</subject><subject>DURCISSEMENT</subject><subject>ENDURECIMIENTO</subject><subject>Enzymes</subject><subject>Gels</subject><subject>GLYCINE MAX</subject><subject>ISOENZIMAS</subject><subject>ISOENZYME</subject><subject>Lignin</subject><subject>PEROXIDASAS</subject><subject>peroxidase</subject><subject>PEROXYDASE</subject><subject>Plant tissues</subject><subject>Plants</subject><subject>Polymerization</subject><subject>PROPIEDADES FISICO-QUIMICAS</subject><subject>PROPRIETE PHYSICOCHIMIQUE</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>seeds</subject><subject>SEMENCE</subject><subject>SEMILLAS</subject><subject>Soybeans</subject><subject>TENEUR EN PROTEINES</subject><subject>TESTA</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNp90T1v2zAQBmCiSBC7aaZuQRFoaobCLo-kKHEMgnwUCJAAqWeCEo8NDUlUSTmI_33p2mi3TCTufe6GO0I-A10CUPF9HJdKLmHJQHwgcyg5W7BS1EdkTmn-07pWM_IxpTWlFDiIEzIDKWUNpZgT_7SJ3vnWTD4MhRlsYfEVuzD2OEymyxXTbZNPRXDF9IJFb9Yh5mrWvi1GjOHNW5OwcDH0f0VCtEUbzLRrueu2rR92bW-fyLEzXcKzw3tKVrc3P6_vFw-Pdz-urx4WrVDltMAGuDVAK1CmrB23vGGOliCYYKxSFJ2UChQHhzUqYS3lVQ1W2gagKTnwU3K5nzvG8HuDadK9Ty12nRkwbJKuOBdKKCWy_PquBElBQL2D3_awjSGliE6P0fcmbjVQvbuBHketpAadb5D1xWHspunR_reHpWfwZQ_WaQrxXy5YxctK5fh8HzsTtPkVfdKrZwWcSsr4H_KWk0Q</recordid><startdate>19910501</startdate><enddate>19910501</enddate><creator>Gillikin, J.W. 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(Bowling Green State University, Bowling Green, OH) ; Graham, J.S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c495t-eb13da10719a58f3d3b2f05142422790ef6691931fe8e94dd03781d6db11b5313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ANION</topic><topic>ANIONES</topic><topic>Cell walls</topic><topic>Cellulose nitrate</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>CONTENIDO PROTEICO</topic><topic>DURCISSEMENT</topic><topic>ENDURECIMIENTO</topic><topic>Enzymes</topic><topic>Gels</topic><topic>GLYCINE MAX</topic><topic>ISOENZIMAS</topic><topic>ISOENZYME</topic><topic>Lignin</topic><topic>PEROXIDASAS</topic><topic>peroxidase</topic><topic>PEROXYDASE</topic><topic>Plant tissues</topic><topic>Plants</topic><topic>Polymerization</topic><topic>PROPIEDADES FISICO-QUIMICAS</topic><topic>PROPRIETE PHYSICOCHIMIQUE</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>seeds</topic><topic>SEMENCE</topic><topic>SEMILLAS</topic><topic>Soybeans</topic><topic>TENEUR EN PROTEINES</topic><topic>TESTA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gillikin, J.W. 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The peroxidase exhibits a pl of 4.1, an apparent molecular mass of 37 kilodaltons, and has properties characteristic of a glycoprotein. The enzyme begins to accumulate approximately 21 days after anthesis and continues to do so throughout the maturation of the seed coat where it can represent at least 5% of the soluble protein in dry seed coats. Due to its localization in the seed, we propose that this isozyme may play a role in the hardening of the seed cost</abstract><cop>United States</cop><pub>American Society of Plant Physiologists</pub><pmid>16668154</pmid><doi>10.1104/pp.96.1.214</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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source | JSTOR Archive Collection A-Z Listing; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ANION ANIONES Cell walls Cellulose nitrate COMPOSICION QUIMICA COMPOSITION CHIMIQUE CONTENIDO PROTEICO DURCISSEMENT ENDURECIMIENTO Enzymes Gels GLYCINE MAX ISOENZIMAS ISOENZYME Lignin PEROXIDASAS peroxidase PEROXYDASE Plant tissues Plants Polymerization PROPIEDADES FISICO-QUIMICAS PROPRIETE PHYSICOCHIMIQUE PROTEINAS PROTEINE PURIFICACION PURIFICATION seeds SEMENCE SEMILLAS Soybeans TENEUR EN PROTEINES TESTA |
title | Purification and developmental analysis of the major anionic peroxidase from the seed coat of Glycine max |
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