Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules
A specific nucleoside diphosphatase was purified from the plant portion of soybean (Glycine max L.) root nodules. This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however,...
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Veröffentlicht in: | Plant physiology (Bethesda) 1988-05, Vol.87 (1), p.41-45 |
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description | A specific nucleoside diphosphatase was purified from the plant portion of soybean (Glycine max L.) root nodules. This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however, hydrolyze any nucleotide disphosphate tested. The pH optimum of the enzyme is about 7.5; it requires a divalent cation for activity; and it is neither inhibited nor activated by any of the metabolites tested. It appears that in vivo this enzyme would be very active, but its function is not clear. |
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This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however, hydrolyze any nucleotide disphosphate tested. The pH optimum of the enzyme is about 7.5; it requires a divalent cation for activity; and it is neither inhibited nor activated by any of the metabolites tested. It appears that in vivo this enzyme would be very active, but its function is not clear.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.87.1.41</identifier><identifier>PMID: 16666123</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>Agronomy. Soil science and plant productions ; Biological and medical sciences ; Chromatography ; Divalent cations ; Economic plant physiology ; ENZIMAS ; ENZYME ; ENZYMES ; EPURATION ; FORMATION DE NODOSITES ; Fundamental and applied biological sciences. Psychology ; GLYCINE MAX ; Metabolism and Enzymology ; NODULACION ; Nodules ; NUCLEOSIDE ; nucleoside-diphosphatase ; NUCLEOSIDES ; NUCLEOSIDOS ; Nucleotides ; Parasitism and symbiosis ; Phosphatases ; Plant physiology and development ; Plants ; PURIFICACION ; PURIFICATION ; ROOT NODULATION ; Root nodules ; roots ; Soybeans ; Symbiosis (nodules, symbiotic nitrogen fixation, mycorrhiza...)</subject><ispartof>Plant physiology (Bethesda), 1988-05, Vol.87 (1), p.41-45</ispartof><rights>Copyright 1988 The American Society of Plant Physiologists</rights><rights>1989 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/4271335$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4271335$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27923,27924,58016,58249</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7095857$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16666123$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Doremus, H.D</creatorcontrib><creatorcontrib>Blevins, D.G</creatorcontrib><title>Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>A specific nucleoside diphosphatase was purified from the plant portion of soybean (Glycine max L.) root nodules. This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however, hydrolyze any nucleotide disphosphate tested. The pH optimum of the enzyme is about 7.5; it requires a divalent cation for activity; and it is neither inhibited nor activated by any of the metabolites tested. It appears that in vivo this enzyme would be very active, but its function is not clear.</description><subject>Agronomy. Soil science and plant productions</subject><subject>Biological and medical sciences</subject><subject>Chromatography</subject><subject>Divalent cations</subject><subject>Economic plant physiology</subject><subject>ENZIMAS</subject><subject>ENZYME</subject><subject>ENZYMES</subject><subject>EPURATION</subject><subject>FORMATION DE NODOSITES</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GLYCINE MAX</subject><subject>Metabolism and Enzymology</subject><subject>NODULACION</subject><subject>Nodules</subject><subject>NUCLEOSIDE</subject><subject>nucleoside-diphosphatase</subject><subject>NUCLEOSIDES</subject><subject>NUCLEOSIDOS</subject><subject>Nucleotides</subject><subject>Parasitism and symbiosis</subject><subject>Phosphatases</subject><subject>Plant physiology and development</subject><subject>Plants</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>ROOT NODULATION</subject><subject>Root nodules</subject><subject>roots</subject><subject>Soybeans</subject><subject>Symbiosis (nodules, symbiotic nitrogen fixation, mycorrhiza...)</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><recordid>eNp90c2L1DAYBvAgijuuXjyKSA6iIMz4vk3SphdBFr9gQUH3HN6myU6WTtNNWmH9680ww6gXc0nI8-MhH4w9Rdgggnw7TRvdbHAj8R5boRLVulJS32crgLIGrdsz9ijnGwBAgfIhO8O6DKzEinXflhR8sDSHOHIae263lMjOLoVfh83oOfE8Obt3fFzs4GIOveN9mLYxT1uaKTvuU9zxHO86RyNPMc58jP0yuPyYPfA0ZPfkOJ-zq48fflx8Xl9-_fTl4v3l2kqAeV37RlWgaup1W3UaoYZOtiBU3zVkayeU1x7b1qKzIDrUBN457TshtahULc7Zu0PvtHQ711s3zokGM6Wwo3RnIgXzbzKGrbmOPw2CknW7L3h9LEjxdnF5NruQrRsGGl1csmmEkK1ALYp89V-JCqGq26rANwdoU8w5OX86DoLZf56ZJqMbg0ZiwS_-vsAfevytAl4eAWVLg0802pBProFWadUU9vzAbvIc0ymWVYNCqBI_O8SeoqHrVBquvmtdXhGU-A2eZ7Vs</recordid><startdate>19880501</startdate><enddate>19880501</enddate><creator>Doremus, H.D</creator><creator>Blevins, D.G</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19880501</creationdate><title>Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules</title><author>Doremus, H.D ; Blevins, D.G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-6f752056ad892b81060b49035db7ac6e35f8f199c1ec03b18a0fee8fb34832563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Agronomy. Soil science and plant productions</topic><topic>Biological and medical sciences</topic><topic>Chromatography</topic><topic>Divalent cations</topic><topic>Economic plant physiology</topic><topic>ENZIMAS</topic><topic>ENZYME</topic><topic>ENZYMES</topic><topic>EPURATION</topic><topic>FORMATION DE NODOSITES</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GLYCINE MAX</topic><topic>Metabolism and Enzymology</topic><topic>NODULACION</topic><topic>Nodules</topic><topic>NUCLEOSIDE</topic><topic>nucleoside-diphosphatase</topic><topic>NUCLEOSIDES</topic><topic>NUCLEOSIDOS</topic><topic>Nucleotides</topic><topic>Parasitism and symbiosis</topic><topic>Phosphatases</topic><topic>Plant physiology and development</topic><topic>Plants</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>ROOT NODULATION</topic><topic>Root nodules</topic><topic>roots</topic><topic>Soybeans</topic><topic>Symbiosis (nodules, symbiotic nitrogen fixation, mycorrhiza...)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Doremus, H.D</creatorcontrib><creatorcontrib>Blevins, D.G</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</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>Doremus, H.D</au><au>Blevins, D.G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1988-05-01</date><risdate>1988</risdate><volume>87</volume><issue>1</issue><spage>41</spage><epage>45</epage><pages>41-45</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>A specific nucleoside diphosphatase was purified from the plant portion of soybean (Glycine max L.) root nodules. This enzyme is highly specific for nucleotide diphosphates; it is unable to hydrolyze nucleotide tri- and monophosphates or a variety of other phosphorylated compounds. It will, however, hydrolyze any nucleotide disphosphate tested. The pH optimum of the enzyme is about 7.5; it requires a divalent cation for activity; and it is neither inhibited nor activated by any of the metabolites tested. It appears that in vivo this enzyme would be very active, but its function is not clear.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>16666123</pmid><doi>10.1104/pp.87.1.41</doi><tpages>5</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 | Agronomy. Soil science and plant productions Biological and medical sciences Chromatography Divalent cations Economic plant physiology ENZIMAS ENZYME ENZYMES EPURATION FORMATION DE NODOSITES Fundamental and applied biological sciences. Psychology GLYCINE MAX Metabolism and Enzymology NODULACION Nodules NUCLEOSIDE nucleoside-diphosphatase NUCLEOSIDES NUCLEOSIDOS Nucleotides Parasitism and symbiosis Phosphatases Plant physiology and development Plants PURIFICACION PURIFICATION ROOT NODULATION Root nodules roots Soybeans Symbiosis (nodules, symbiotic nitrogen fixation, mycorrhiza...) |
title | Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules |
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