Nitrate reductase-deficient mutants in barley: enzyme stability and peptide mapping
Thermal stability and pH optima of NADH-nitrate reductase-associated cytochrome c reductase and FMNH 2-nitrate reductase from wild type, cv Steptoe or Winer, and mutants nar 1d, nar 1g, nar 1h, Xno 18 and Xno 19 were compared to determine if structural differences in the nitrate reductase protein co...
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| Veröffentlicht in: | Phytochemistry (Oxford) 1984, Vol.23 (2), p.229-232 |
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| creator | Min Kuo, Tsung Kleinhofs, Andris Somers, David A. Warner, Robert L. |
| description | Thermal stability and pH optima of NADH-nitrate reductase-associated cytochrome
c reductase and FMNH
2-nitrate reductase from wild type, cv Steptoe or Winer, and mutants
nar 1d,
nar 1g,
nar 1h, Xno 18 and Xno 19 were compared to determine if structural differences in the nitrate reductase protein could be detected. Also, the nitrate reductase-associated cytochrome
c reductase from
nar 1d was purified and compared with the wild type by peptide mapping. The pH optimum for FMNH
2-nitrate reductase from Steptoe and
nar 1h, and for NADH-cytochrome
c reductase from Steptoe,
nar 1d,
nar 1g and
nar 2a was 7.5. Thermal stabilities of the nitrate reductase-associated activities (FMNH
2-nitrate reductase or NADH-cytochrome
c reductase) from
nar mutants were less than the Steptoe wild type, while Xno mutants were equal to the Winer wild type. Cleveland peptide maps of
nar 1d NADH-cytochrome
c reductase and Steptoe nitrate reductase were identicalwhen digested with endoprotease lys-C but were distinctly different in one peptide when digested with
Staphylococcus aureus endoprotease V8. These results provide evidence that
nar 1 gene codes for the nitrate reductase polypeptide. |
| doi_str_mv | 10.1016/S0031-9422(00)80307-6 |
| format | Article |
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c reductase and FMNH
2-nitrate reductase from wild type, cv Steptoe or Winer, and mutants
nar 1d,
nar 1g,
nar 1h, Xno 18 and Xno 19 were compared to determine if structural differences in the nitrate reductase protein could be detected. Also, the nitrate reductase-associated cytochrome
c reductase from
nar 1d was purified and compared with the wild type by peptide mapping. The pH optimum for FMNH
2-nitrate reductase from Steptoe and
nar 1h, and for NADH-cytochrome
c reductase from Steptoe,
nar 1d,
nar 1g and
nar 2a was 7.5. Thermal stabilities of the nitrate reductase-associated activities (FMNH
2-nitrate reductase or NADH-cytochrome
c reductase) from
nar mutants were less than the Steptoe wild type, while Xno mutants were equal to the Winer wild type. Cleveland peptide maps of
nar 1d NADH-cytochrome
c reductase and Steptoe nitrate reductase were identicalwhen digested with endoprotease lys-C but were distinctly different in one peptide when digested with
Staphylococcus aureus endoprotease V8. These results provide evidence that
nar 1 gene codes for the nitrate reductase polypeptide.</description><identifier>ISSN: 0031-9422</identifier><identifier>EISSN: 1873-3700</identifier><identifier>DOI: 10.1016/S0031-9422(00)80307-6</identifier><language>eng</language><publisher>Amsterdam: Elsevier Ltd</publisher><subject>Analytical, structural and metabolic biochemistry ; barley ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Gramineae ; Hordeum vulgare ; mutants ; nitrate reductase ; nitrate reductase (NADH) ; Oxidoreductases ; peptide mapping ; stability</subject><ispartof>Phytochemistry (Oxford), 1984, Vol.23 (2), p.229-232</ispartof><rights>1984</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-74efdc86fdeef84d25bacf4b359e8f665b006555f7a165248f9460980ab86b0c3</citedby><cites>FETCH-LOGICAL-c391t-74efdc86fdeef84d25bacf4b359e8f665b006555f7a165248f9460980ab86b0c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0031942200803076$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9513531$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Min Kuo, Tsung</creatorcontrib><creatorcontrib>Kleinhofs, Andris</creatorcontrib><creatorcontrib>Somers, David A.</creatorcontrib><creatorcontrib>Warner, Robert L.</creatorcontrib><title>Nitrate reductase-deficient mutants in barley: enzyme stability and peptide mapping</title><title>Phytochemistry (Oxford)</title><description>Thermal stability and pH optima of NADH-nitrate reductase-associated cytochrome
c reductase and FMNH
2-nitrate reductase from wild type, cv Steptoe or Winer, and mutants
nar 1d,
nar 1g,
nar 1h, Xno 18 and Xno 19 were compared to determine if structural differences in the nitrate reductase protein could be detected. Also, the nitrate reductase-associated cytochrome
c reductase from
nar 1d was purified and compared with the wild type by peptide mapping. The pH optimum for FMNH
2-nitrate reductase from Steptoe and
nar 1h, and for NADH-cytochrome
c reductase from Steptoe,
nar 1d,
nar 1g and
nar 2a was 7.5. Thermal stabilities of the nitrate reductase-associated activities (FMNH
2-nitrate reductase or NADH-cytochrome
c reductase) from
nar mutants were less than the Steptoe wild type, while Xno mutants were equal to the Winer wild type. Cleveland peptide maps of
nar 1d NADH-cytochrome
c reductase and Steptoe nitrate reductase were identicalwhen digested with endoprotease lys-C but were distinctly different in one peptide when digested with
Staphylococcus aureus endoprotease V8. These results provide evidence that
nar 1 gene codes for the nitrate reductase polypeptide.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>barley</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gramineae</subject><subject>Hordeum vulgare</subject><subject>mutants</subject><subject>nitrate reductase</subject><subject>nitrate reductase (NADH)</subject><subject>Oxidoreductases</subject><subject>peptide mapping</subject><subject>stability</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><recordid>eNqF0M9rFTEQwPEgFny2_gliDiL1sHay2WSzXkSK2kKxh2fPYTaZlMj-MskTnn999_WVXj3N5TPJ8GXsrYBPAoS-2AJIUXVNXZ8DfDQgoa30C7YRppWVbAFess0zecVe5_wbAJTSesO2P2NJWIgn8jtXMFPlKUQXaSp83BWcSuZx4j2mgfafOU3_9iPxXLCPQyx7jpPnCy0leuIjLkuc7s_YScAh05unecruvn_7dXlV3dz-uL78elM52YlStQ0F74wOniiYxteqRxeaXqqOTNBa9QBaKRVaFFrVjQldo6EzgL3RPTh5yj4c313S_GdHudgxZkfDgBPNu2yFNBJkBytUR-jSnHOiYJcUR0x7K8AeEtrHhPbQxwLYx4RWr3vvnz7A7HAICScX8_Nyp4RUUqzs3ZEFnC3ep5XcbWsQEmolO2kO4stR0Jrjb6Rk86GwIx8TuWL9HP9zygO-kY8n</recordid><startdate>1984</startdate><enddate>1984</enddate><creator>Min Kuo, Tsung</creator><creator>Kleinhofs, Andris</creator><creator>Somers, David A.</creator><creator>Warner, Robert L.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>1984</creationdate><title>Nitrate reductase-deficient mutants in barley: enzyme stability and peptide mapping</title><author>Min Kuo, Tsung ; Kleinhofs, Andris ; Somers, David A. ; Warner, Robert L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-74efdc86fdeef84d25bacf4b359e8f665b006555f7a165248f9460980ab86b0c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>barley</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gramineae</topic><topic>Hordeum vulgare</topic><topic>mutants</topic><topic>nitrate reductase</topic><topic>nitrate reductase (NADH)</topic><topic>Oxidoreductases</topic><topic>peptide mapping</topic><topic>stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Min Kuo, Tsung</creatorcontrib><creatorcontrib>Kleinhofs, Andris</creatorcontrib><creatorcontrib>Somers, David A.</creatorcontrib><creatorcontrib>Warner, Robert L.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Min Kuo, Tsung</au><au>Kleinhofs, Andris</au><au>Somers, David A.</au><au>Warner, Robert L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nitrate reductase-deficient mutants in barley: enzyme stability and peptide mapping</atitle><jtitle>Phytochemistry (Oxford)</jtitle><date>1984</date><risdate>1984</risdate><volume>23</volume><issue>2</issue><spage>229</spage><epage>232</epage><pages>229-232</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><abstract>Thermal stability and pH optima of NADH-nitrate reductase-associated cytochrome
c reductase and FMNH
2-nitrate reductase from wild type, cv Steptoe or Winer, and mutants
nar 1d,
nar 1g,
nar 1h, Xno 18 and Xno 19 were compared to determine if structural differences in the nitrate reductase protein could be detected. Also, the nitrate reductase-associated cytochrome
c reductase from
nar 1d was purified and compared with the wild type by peptide mapping. The pH optimum for FMNH
2-nitrate reductase from Steptoe and
nar 1h, and for NADH-cytochrome
c reductase from Steptoe,
nar 1d,
nar 1g and
nar 2a was 7.5. Thermal stabilities of the nitrate reductase-associated activities (FMNH
2-nitrate reductase or NADH-cytochrome
c reductase) from
nar mutants were less than the Steptoe wild type, while Xno mutants were equal to the Winer wild type. Cleveland peptide maps of
nar 1d NADH-cytochrome
c reductase and Steptoe nitrate reductase were identicalwhen digested with endoprotease lys-C but were distinctly different in one peptide when digested with
Staphylococcus aureus endoprotease V8. These results provide evidence that
nar 1 gene codes for the nitrate reductase polypeptide.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><doi>10.1016/S0031-9422(00)80307-6</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0031-9422 |
| ispartof | Phytochemistry (Oxford), 1984, Vol.23 (2), p.229-232 |
| issn | 0031-9422 1873-3700 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_13830390 |
| source | Elsevier ScienceDirect Journals |
| subjects | Analytical, structural and metabolic biochemistry barley Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gramineae Hordeum vulgare mutants nitrate reductase nitrate reductase (NADH) Oxidoreductases peptide mapping stability |
| title | Nitrate reductase-deficient mutants in barley: enzyme stability and peptide mapping |
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