Purification and Molecular Analysis of an Extracellular γ-Glutamyl Hydrolase Present in Young Tissues of the Soybean Plant
A polypeptide present in intercellular wash fluids of young leaves ofGlycine maxhas been purified to electrophoretic homogeneity. The protein has been identified as γ-glutamyl hydrolase (GGH) based on the shared homology with a recently cloned cDNA from rat. The enzyme is present within the extracel...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1996-11, Vol.228 (1), p.1-6 |
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| creator | Huangpu, J. Pak, J.H. Graham, M.C. Rickle, S.A. Graham, J.S. |
| description | A polypeptide present in intercellular wash fluids of young leaves ofGlycine maxhas been purified to electrophoretic homogeneity. The protein has been identified as γ-glutamyl hydrolase (GGH) based on the shared homology with a recently cloned cDNA from rat. The enzyme is present within the extracellular space of young leaves and a portion is bound to the cell wall. Northern and Western analysis confirm that this polypeptide is expressed only in young (1-15 d old) leaf, stem and root tissue and is therefore expressed under a strict developmental program. The primary sequence of γ-glutamyl hydrolase shares amino acid identity with a cDNA clone from rat and two partially sequenced cDNAs fromArabidopsis.Although the completein vivofunction of γ-glutamyl hydrolase in plants is unclear, it is known that the protein plays a critical role in folate metabolism and therefore likely in meeting the physiological demands of growing plant tissues. |
| doi_str_mv | 10.1006/bbrc.1996.1608 |
| format | Article |
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The protein has been identified as γ-glutamyl hydrolase (GGH) based on the shared homology with a recently cloned cDNA from rat. The enzyme is present within the extracellular space of young leaves and a portion is bound to the cell wall. Northern and Western analysis confirm that this polypeptide is expressed only in young (1-15 d old) leaf, stem and root tissue and is therefore expressed under a strict developmental program. The primary sequence of γ-glutamyl hydrolase shares amino acid identity with a cDNA clone from rat and two partially sequenced cDNAs fromArabidopsis.Although the completein vivofunction of γ-glutamyl hydrolase in plants is unclear, it is known that the protein plays a critical role in folate metabolism and therefore likely in meeting the physiological demands of growing plant tissues.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1996.1608</identifier><identifier>PMID: 8912628</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Blotting, Western ; Cell Wall - enzymology ; Cross Reactions ; DNA, Complementary - genetics ; FEUILLE ; gamma-Glutamyl Hydrolase - chemistry ; gamma-Glutamyl Hydrolase - genetics ; gamma-Glutamyl Hydrolase - isolation & purification ; gamma-Glutamyl Hydrolase - metabolism ; Gene Expression ; GENETICA MOLECULAR ; GENETIQUE MOLECULAIRE ; GLYCINE MAX ; Glycine max - enzymology ; HIDROLASAS ; HOJAS ; HYDROLASE ; Metalloendopeptidases - immunology ; Molecular Sequence Data ; PARED CELULAR ; PAROI CELLULAIRE ; PEPTIDASAS ; PEPTIDASE ; PEPTIDE ; PEPTIDOS ; Plant Leaves - enzymology ; PURIFICACION ; PURIFICATION ; RACINE ; RAICES ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNA, Plant - genetics ; RNA, Plant - metabolism ; TALLO ; TIGE</subject><ispartof>Biochemical and biophysical research communications, 1996-11, Vol.228 (1), p.1-6</ispartof><rights>1996 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c358t-d03b51f231bca0e15ed0fc752c35c6c75bd227a7cd129333d45119cf077b0c483</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.1996.1608$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8912628$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Huangpu, J.</creatorcontrib><creatorcontrib>Pak, J.H.</creatorcontrib><creatorcontrib>Graham, M.C.</creatorcontrib><creatorcontrib>Rickle, S.A.</creatorcontrib><creatorcontrib>Graham, J.S.</creatorcontrib><title>Purification and Molecular Analysis of an Extracellular γ-Glutamyl Hydrolase Present in Young Tissues of the Soybean Plant</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>A polypeptide present in intercellular wash fluids of young leaves ofGlycine maxhas been purified to electrophoretic homogeneity. The protein has been identified as γ-glutamyl hydrolase (GGH) based on the shared homology with a recently cloned cDNA from rat. The enzyme is present within the extracellular space of young leaves and a portion is bound to the cell wall. Northern and Western analysis confirm that this polypeptide is expressed only in young (1-15 d old) leaf, stem and root tissue and is therefore expressed under a strict developmental program. The primary sequence of γ-glutamyl hydrolase shares amino acid identity with a cDNA clone from rat and two partially sequenced cDNAs fromArabidopsis.Although the completein vivofunction of γ-glutamyl hydrolase in plants is unclear, it is known that the protein plays a critical role in folate metabolism and therefore likely in meeting the physiological demands of growing plant tissues.</description><subject>Blotting, Western</subject><subject>Cell Wall - enzymology</subject><subject>Cross Reactions</subject><subject>DNA, Complementary - genetics</subject><subject>FEUILLE</subject><subject>gamma-Glutamyl Hydrolase - chemistry</subject><subject>gamma-Glutamyl Hydrolase - genetics</subject><subject>gamma-Glutamyl Hydrolase - isolation & purification</subject><subject>gamma-Glutamyl Hydrolase - metabolism</subject><subject>Gene Expression</subject><subject>GENETICA MOLECULAR</subject><subject>GENETIQUE MOLECULAIRE</subject><subject>GLYCINE MAX</subject><subject>Glycine max - enzymology</subject><subject>HIDROLASAS</subject><subject>HOJAS</subject><subject>HYDROLASE</subject><subject>Metalloendopeptidases - immunology</subject><subject>Molecular Sequence Data</subject><subject>PARED CELULAR</subject><subject>PAROI CELLULAIRE</subject><subject>PEPTIDASAS</subject><subject>PEPTIDASE</subject><subject>PEPTIDE</subject><subject>PEPTIDOS</subject><subject>Plant Leaves - enzymology</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>RACINE</subject><subject>RAICES</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA, Plant - genetics</subject><subject>RNA, Plant - metabolism</subject><subject>TALLO</subject><subject>TIGE</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1rFTEUhoNY6rW6dSEIWbmb25zMZ5al1Fao9EJb0FXIJGdqJHdSk0xx8Gf5P_xNZu69dOcqgefNe3IeQt4BWwNjzWnfB70GIZo1NKx7QVbABCs4sOolWbGcKLiAr6_I6xh_MAZQNeKYHHcCeMO7Ffm9mYIdrFbJ-pGq0dAv3qGenAr0bFRujjZSP2RCL36loDQ6t4N__xSXbkpqOzt6NZvgnYpINwEjjonakX7z0_hA72yME-4q0nekt37uMXdtnBrTG3I0KBfx7eE8IfefLu7Or4rrm8vP52fXhS7rLhWGlX0NAy-h14oh1GjYoNuaZ6ybfOkN561qtQEuyrI0VQ0g9MDatme66soT8nHf-xj8z_yZJLc2LouoEf0UZdvVvOrqJgfX-6AOPsaAg3wMdqvCLIHJxbZcbMvFtlxs5wcfDs1Tv0XzHD_ozfz9ng_KS_UQbJT3t6JlUO6mdXuIefcni0FGbXHUaGxAnaTx9n9z_wHiiJjE</recordid><startdate>19961101</startdate><enddate>19961101</enddate><creator>Huangpu, J.</creator><creator>Pak, J.H.</creator><creator>Graham, M.C.</creator><creator>Rickle, S.A.</creator><creator>Graham, J.S.</creator><general>Elsevier Inc</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19961101</creationdate><title>Purification and Molecular Analysis of an Extracellular γ-Glutamyl Hydrolase Present in Young Tissues of the Soybean Plant</title><author>Huangpu, J. ; Pak, J.H. ; Graham, M.C. ; Rickle, S.A. ; Graham, J.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c358t-d03b51f231bca0e15ed0fc752c35c6c75bd227a7cd129333d45119cf077b0c483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Blotting, Western</topic><topic>Cell Wall - enzymology</topic><topic>Cross Reactions</topic><topic>DNA, Complementary - genetics</topic><topic>FEUILLE</topic><topic>gamma-Glutamyl Hydrolase - chemistry</topic><topic>gamma-Glutamyl Hydrolase - genetics</topic><topic>gamma-Glutamyl Hydrolase - isolation & purification</topic><topic>gamma-Glutamyl Hydrolase - metabolism</topic><topic>Gene Expression</topic><topic>GENETICA MOLECULAR</topic><topic>GENETIQUE MOLECULAIRE</topic><topic>GLYCINE MAX</topic><topic>Glycine max - enzymology</topic><topic>HIDROLASAS</topic><topic>HOJAS</topic><topic>HYDROLASE</topic><topic>Metalloendopeptidases - immunology</topic><topic>Molecular Sequence Data</topic><topic>PARED CELULAR</topic><topic>PAROI CELLULAIRE</topic><topic>PEPTIDASAS</topic><topic>PEPTIDASE</topic><topic>PEPTIDE</topic><topic>PEPTIDOS</topic><topic>Plant Leaves - enzymology</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>RACINE</topic><topic>RAICES</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA, Plant - genetics</topic><topic>RNA, Plant - metabolism</topic><topic>TALLO</topic><topic>TIGE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huangpu, J.</creatorcontrib><creatorcontrib>Pak, J.H.</creatorcontrib><creatorcontrib>Graham, M.C.</creatorcontrib><creatorcontrib>Rickle, S.A.</creatorcontrib><creatorcontrib>Graham, J.S.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huangpu, J.</au><au>Pak, J.H.</au><au>Graham, M.C.</au><au>Rickle, S.A.</au><au>Graham, J.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Molecular Analysis of an Extracellular γ-Glutamyl Hydrolase Present in Young Tissues of the Soybean Plant</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1996-11-01</date><risdate>1996</risdate><volume>228</volume><issue>1</issue><spage>1</spage><epage>6</epage><pages>1-6</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>A polypeptide present in intercellular wash fluids of young leaves ofGlycine maxhas been purified to electrophoretic homogeneity. The protein has been identified as γ-glutamyl hydrolase (GGH) based on the shared homology with a recently cloned cDNA from rat. The enzyme is present within the extracellular space of young leaves and a portion is bound to the cell wall. Northern and Western analysis confirm that this polypeptide is expressed only in young (1-15 d old) leaf, stem and root tissue and is therefore expressed under a strict developmental program. The primary sequence of γ-glutamyl hydrolase shares amino acid identity with a cDNA clone from rat and two partially sequenced cDNAs fromArabidopsis.Although the completein vivofunction of γ-glutamyl hydrolase in plants is unclear, it is known that the protein plays a critical role in folate metabolism and therefore likely in meeting the physiological demands of growing plant tissues.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8912628</pmid><doi>10.1006/bbrc.1996.1608</doi><tpages>6</tpages></addata></record> |
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| subjects | Blotting, Western Cell Wall - enzymology Cross Reactions DNA, Complementary - genetics FEUILLE gamma-Glutamyl Hydrolase - chemistry gamma-Glutamyl Hydrolase - genetics gamma-Glutamyl Hydrolase - isolation & purification gamma-Glutamyl Hydrolase - metabolism Gene Expression GENETICA MOLECULAR GENETIQUE MOLECULAIRE GLYCINE MAX Glycine max - enzymology HIDROLASAS HOJAS HYDROLASE Metalloendopeptidases - immunology Molecular Sequence Data PARED CELULAR PAROI CELLULAIRE PEPTIDASAS PEPTIDASE PEPTIDE PEPTIDOS Plant Leaves - enzymology PURIFICACION PURIFICATION RACINE RAICES RNA, Messenger - genetics RNA, Messenger - metabolism RNA, Plant - genetics RNA, Plant - metabolism TALLO TIGE |
| title | Purification and Molecular Analysis of an Extracellular γ-Glutamyl Hydrolase Present in Young Tissues of the Soybean Plant |
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