Production of a monocot-specific monoclonal antibody against acetohydroxyacid synthase and its use in the purification and characterization of the enzyme
Acetohydroxyacid synthase [AHAS; acetolactate pyruvate-lyase (carboxylating). EC 4.1.3.18], the first enzyme unique to the biosynthesis of valine, leucine, and isoleucine, is a known target for several different chemical classes of herbicides. Antibodies required for immunological characterization o...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1991-06, Vol.88 (11), p.4572-4576 |
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| creator | Singh, Bijay K. Lumanglas, Araceli Wang, Bosco Shang |
| description | Acetohydroxyacid synthase [AHAS; acetolactate pyruvate-lyase (carboxylating). EC 4.1.3.18], the first enzyme unique to the biosynthesis of valine, leucine, and isoleucine, is a known target for several different chemical classes of herbicides. Antibodies required for immunological characterization of the enzyme have not been generated by the conventional method of antibody production using purified protein. Monoclonal antibodies were raised against AHAS from corn by using as immunogen a synthetic peptide representing this enzyme. This antibody immunoprecipitated the enzyme activity from corn. On a Western blot, a protein band with a molecular weight of 65,000 was detected in crude extracts of corn. Furthermore, a monoclonal antibody immunoaffinity gel was used to isolate a single protein from crude enzyme preparations that migrated at Mr, 65,000 in an SDS/polyacrylamide gel. The molecular weight of this protein band is the molecular weight predicted for a plant AHAS from a cloned gene sequence. These results strongly suggest that the Mr 65,000 protein represents AHAS in corn extracts. Interestingly, the monoclonal antibody specifically recognized the enzyme from monocots and did not crossreact with AHAS from any dicot species tested. Identification of this monoclonal antibody that distinguishes monocot and dicot AHAS is significant because of a very high degree of amino acid conservation (85%) between AHAS proteins from different species. |
| doi_str_mv | 10.1073/pnas.88.11.4572 |
| format | Article |
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Faculty of Agriculture ; American Cyanamid Company, Princeton, NJ</creatorcontrib><description>Acetohydroxyacid synthase [AHAS; acetolactate pyruvate-lyase (carboxylating). EC 4.1.3.18], the first enzyme unique to the biosynthesis of valine, leucine, and isoleucine, is a known target for several different chemical classes of herbicides. Antibodies required for immunological characterization of the enzyme have not been generated by the conventional method of antibody production using purified protein. Monoclonal antibodies were raised against AHAS from corn by using as immunogen a synthetic peptide representing this enzyme. This antibody immunoprecipitated the enzyme activity from corn. On a Western blot, a protein band with a molecular weight of 65,000 was detected in crude extracts of corn. Furthermore, a monoclonal antibody immunoaffinity gel was used to isolate a single protein from crude enzyme preparations that migrated at Mr, 65,000 in an SDS/polyacrylamide gel. The molecular weight of this protein band is the molecular weight predicted for a plant AHAS from a cloned gene sequence. These results strongly suggest that the Mr 65,000 protein represents AHAS in corn extracts. Interestingly, the monoclonal antibody specifically recognized the enzyme from monocots and did not crossreact with AHAS from any dicot species tested. Identification of this monoclonal antibody that distinguishes monocot and dicot AHAS is significant because of a very high degree of amino acid conservation (85%) between AHAS proteins from different species.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.88.11.4572</identifier><identifier>PMID: 2052541</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>acetohydroxyacid synthase ; Acetolactate Synthase - genetics ; Acetolactate Synthase - immunology ; Acetolactate Synthase - isolation & purification ; actividad enzimatica ; activite enzymatique ; Amino Acid Sequence ; Amino acids ; Analytical, structural and metabolic biochemistry ; Animals ; Antibodies ; Antibodies, Monoclonal ; anticorps monoclonal ; anticuerpos monoclonales ; Antigen-Antibody Complex ; Biological and medical sciences ; biosintesis ; biosynthese ; biosynthesis ; Blotting, Western ; Chromatography, Gel ; Corn ; cultivo protegido ; culture sous abri ; enzyme inhibitors ; Enzyme linked immunosorbent assay ; Enzymes ; Enzymes and enzyme inhibitors ; enzymic activity ; Fundamental and applied biological sciences. Psychology ; Gels ; greenhouses ; herbicidas ; herbicide ; herbicides ; immunoprecipitation tests ; inhibidores de enzimas ; inhibiteur d' enzyme ; invernaderos ; liasas ; lyase ; Lyases ; Mice ; Mice, Inbred BALB C - immunology ; Molecular Sequence Data ; Molecular weight ; Monoclonal antibodies ; monocotiledoneas ; monocotyledone ; monocotyledons ; peptide ; peptides ; Peptides - chemical synthesis ; peptidos ; Plants ; Plants - enzymology ; protected cultivation ; Protein Conformation ; Proteins ; purificacion ; purification ; reaccion de inmunoprecipitacion ; reaction d' immunoprecipitation ; Sequence Homology, Nucleic Acid ; serre ; Species Specificity ; Zea mays</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1991-06, Vol.88 (11), p.4572-4576</ispartof><rights>Copyright 1991 The National Academy of Sciences of the United States of America</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c546t-a93bd88d7503e3d761ca4e6fd42235349277f88035fae70bb340870fef252e9d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/88/11.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2357094$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2357094$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19771665$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2052541$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Singh, Bijay K.</creatorcontrib><creatorcontrib>Lumanglas, Araceli</creatorcontrib><creatorcontrib>Wang, Bosco Shang</creatorcontrib><creatorcontrib>Zagazig Univ., Moshtohor (Egypt). Faculty of Agriculture</creatorcontrib><creatorcontrib>American Cyanamid Company, Princeton, NJ</creatorcontrib><title>Production of a monocot-specific monoclonal antibody against acetohydroxyacid synthase and its use in the purification and characterization of the enzyme</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Acetohydroxyacid synthase [AHAS; acetolactate pyruvate-lyase (carboxylating). EC 4.1.3.18], the first enzyme unique to the biosynthesis of valine, leucine, and isoleucine, is a known target for several different chemical classes of herbicides. Antibodies required for immunological characterization of the enzyme have not been generated by the conventional method of antibody production using purified protein. Monoclonal antibodies were raised against AHAS from corn by using as immunogen a synthetic peptide representing this enzyme. This antibody immunoprecipitated the enzyme activity from corn. On a Western blot, a protein band with a molecular weight of 65,000 was detected in crude extracts of corn. Furthermore, a monoclonal antibody immunoaffinity gel was used to isolate a single protein from crude enzyme preparations that migrated at Mr, 65,000 in an SDS/polyacrylamide gel. The molecular weight of this protein band is the molecular weight predicted for a plant AHAS from a cloned gene sequence. These results strongly suggest that the Mr 65,000 protein represents AHAS in corn extracts. Interestingly, the monoclonal antibody specifically recognized the enzyme from monocots and did not crossreact with AHAS from any dicot species tested. Identification of this monoclonal antibody that distinguishes monocot and dicot AHAS is significant because of a very high degree of amino acid conservation (85%) between AHAS proteins from different species.</description><subject>acetohydroxyacid synthase</subject><subject>Acetolactate Synthase - genetics</subject><subject>Acetolactate Synthase - immunology</subject><subject>Acetolactate Synthase - isolation & purification</subject><subject>actividad enzimatica</subject><subject>activite enzymatique</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Monoclonal</subject><subject>anticorps monoclonal</subject><subject>anticuerpos monoclonales</subject><subject>Antigen-Antibody Complex</subject><subject>Biological and medical sciences</subject><subject>biosintesis</subject><subject>biosynthese</subject><subject>biosynthesis</subject><subject>Blotting, Western</subject><subject>Chromatography, Gel</subject><subject>Corn</subject><subject>cultivo protegido</subject><subject>culture sous abri</subject><subject>enzyme inhibitors</subject><subject>Enzyme linked immunosorbent assay</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>enzymic activity</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>greenhouses</subject><subject>herbicidas</subject><subject>herbicide</subject><subject>herbicides</subject><subject>immunoprecipitation tests</subject><subject>inhibidores de enzimas</subject><subject>inhibiteur d' enzyme</subject><subject>invernaderos</subject><subject>liasas</subject><subject>lyase</subject><subject>Lyases</subject><subject>Mice</subject><subject>Mice, Inbred BALB C - immunology</subject><subject>Molecular Sequence Data</subject><subject>Molecular weight</subject><subject>Monoclonal antibodies</subject><subject>monocotiledoneas</subject><subject>monocotyledone</subject><subject>monocotyledons</subject><subject>peptide</subject><subject>peptides</subject><subject>Peptides - chemical synthesis</subject><subject>peptidos</subject><subject>Plants</subject><subject>Plants - enzymology</subject><subject>protected cultivation</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>purificacion</subject><subject>purification</subject><subject>reaccion de inmunoprecipitacion</subject><subject>reaction d' immunoprecipitation</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>serre</subject><subject>Species Specificity</subject><subject>Zea mays</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhSMEKsPAmg2gbIBVpn7EsS11gypeUiWQoGvrjmPPuMrYg-2gpv-Ef0vCpB26gZUtn-_ec6xTFM8xWmHE6eneQ1oJscJ4VTNOHhQLjCSumlqih8UCIcIrUZP6cfEkpSuEkGQCnRQnBDHCarwofn2Noe11dsGXwZZQ7oIPOuQq7Y121unDQxc8dCX47NahHUrYgPMpl6BNDtuhjeF6AO3aMg0-byGZEW1Ll1PZj3fny7w15b6P00L44zXpegsRdDbR3cBtgAk0_mbYmafFIwtdMs_mc1lcfnj__fxTdfHl4-fzdxeVZnWTK5B03QrRcoaooS1vsIbaNLatCaGM1pJwboVAlFkwHK3XtEaCI2ssYcTIli6Ls8Pefb_emVYbnyN0ah_dDuKgAjh1X_Fuqzbhp2KYjw0sizfzeAw_epOy2rmkTdeBN6FPSqCGYiLZf0HcEEG5nDaeHkAdQ0rR2LssGKmpdDWVroRQGKup9HHi5d9fuOPnlkf99axD0tDZCF67dFwrOcdNM0V8NXOTwa18z-jtPwFl-67L5jqP5IsDeZVyiMdElHEk66OThaBgE8c0l9-wlBghLrHE9DdC-OTG</recordid><startdate>19910601</startdate><enddate>19910601</enddate><creator>Singh, Bijay K.</creator><creator>Lumanglas, Araceli</creator><creator>Wang, Bosco Shang</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</scope><scope>IQODW</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>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>19910601</creationdate><title>Production of a monocot-specific monoclonal antibody against acetohydroxyacid synthase and its use in the purification and characterization of the enzyme</title><author>Singh, Bijay K. ; Lumanglas, Araceli ; Wang, Bosco Shang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c546t-a93bd88d7503e3d761ca4e6fd42235349277f88035fae70bb340870fef252e9d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>acetohydroxyacid synthase</topic><topic>Acetolactate Synthase - genetics</topic><topic>Acetolactate Synthase - immunology</topic><topic>Acetolactate Synthase - isolation & purification</topic><topic>actividad enzimatica</topic><topic>activite enzymatique</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Monoclonal</topic><topic>anticorps monoclonal</topic><topic>anticuerpos monoclonales</topic><topic>Antigen-Antibody Complex</topic><topic>Biological and medical sciences</topic><topic>biosintesis</topic><topic>biosynthese</topic><topic>biosynthesis</topic><topic>Blotting, Western</topic><topic>Chromatography, Gel</topic><topic>Corn</topic><topic>cultivo protegido</topic><topic>culture sous abri</topic><topic>enzyme inhibitors</topic><topic>Enzyme linked immunosorbent assay</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>enzymic activity</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>greenhouses</topic><topic>herbicidas</topic><topic>herbicide</topic><topic>herbicides</topic><topic>immunoprecipitation tests</topic><topic>inhibidores de enzimas</topic><topic>inhibiteur d' enzyme</topic><topic>invernaderos</topic><topic>liasas</topic><topic>lyase</topic><topic>Lyases</topic><topic>Mice</topic><topic>Mice, Inbred BALB C - immunology</topic><topic>Molecular Sequence Data</topic><topic>Molecular weight</topic><topic>Monoclonal antibodies</topic><topic>monocotiledoneas</topic><topic>monocotyledone</topic><topic>monocotyledons</topic><topic>peptide</topic><topic>peptides</topic><topic>Peptides - chemical synthesis</topic><topic>peptidos</topic><topic>Plants</topic><topic>Plants - enzymology</topic><topic>protected cultivation</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>purificacion</topic><topic>purification</topic><topic>reaccion de inmunoprecipitacion</topic><topic>reaction d' immunoprecipitation</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>serre</topic><topic>Species Specificity</topic><topic>Zea mays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Singh, Bijay K.</creatorcontrib><creatorcontrib>Lumanglas, Araceli</creatorcontrib><creatorcontrib>Wang, Bosco Shang</creatorcontrib><creatorcontrib>Zagazig Univ., Moshtohor (Egypt). Faculty of Agriculture</creatorcontrib><creatorcontrib>American Cyanamid Company, Princeton, NJ</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</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>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Singh, Bijay K.</au><au>Lumanglas, Araceli</au><au>Wang, Bosco Shang</au><aucorp>Zagazig Univ., Moshtohor (Egypt). Faculty of Agriculture</aucorp><aucorp>American Cyanamid Company, Princeton, NJ</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production of a monocot-specific monoclonal antibody against acetohydroxyacid synthase and its use in the purification and characterization of the enzyme</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1991-06-01</date><risdate>1991</risdate><volume>88</volume><issue>11</issue><spage>4572</spage><epage>4576</epage><pages>4572-4576</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Acetohydroxyacid synthase [AHAS; acetolactate pyruvate-lyase (carboxylating). EC 4.1.3.18], the first enzyme unique to the biosynthesis of valine, leucine, and isoleucine, is a known target for several different chemical classes of herbicides. Antibodies required for immunological characterization of the enzyme have not been generated by the conventional method of antibody production using purified protein. Monoclonal antibodies were raised against AHAS from corn by using as immunogen a synthetic peptide representing this enzyme. This antibody immunoprecipitated the enzyme activity from corn. On a Western blot, a protein band with a molecular weight of 65,000 was detected in crude extracts of corn. Furthermore, a monoclonal antibody immunoaffinity gel was used to isolate a single protein from crude enzyme preparations that migrated at Mr, 65,000 in an SDS/polyacrylamide gel. The molecular weight of this protein band is the molecular weight predicted for a plant AHAS from a cloned gene sequence. These results strongly suggest that the Mr 65,000 protein represents AHAS in corn extracts. Interestingly, the monoclonal antibody specifically recognized the enzyme from monocots and did not crossreact with AHAS from any dicot species tested. Identification of this monoclonal antibody that distinguishes monocot and dicot AHAS is significant because of a very high degree of amino acid conservation (85%) between AHAS proteins from different species.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2052541</pmid><doi>10.1073/pnas.88.11.4572</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1991-06, Vol.88 (11), p.4572-4576 |
| issn | 0027-8424 1091-6490 |
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| subjects | acetohydroxyacid synthase Acetolactate Synthase - genetics Acetolactate Synthase - immunology Acetolactate Synthase - isolation & purification actividad enzimatica activite enzymatique Amino Acid Sequence Amino acids Analytical, structural and metabolic biochemistry Animals Antibodies Antibodies, Monoclonal anticorps monoclonal anticuerpos monoclonales Antigen-Antibody Complex Biological and medical sciences biosintesis biosynthese biosynthesis Blotting, Western Chromatography, Gel Corn cultivo protegido culture sous abri enzyme inhibitors Enzyme linked immunosorbent assay Enzymes Enzymes and enzyme inhibitors enzymic activity Fundamental and applied biological sciences. Psychology Gels greenhouses herbicidas herbicide herbicides immunoprecipitation tests inhibidores de enzimas inhibiteur d' enzyme invernaderos liasas lyase Lyases Mice Mice, Inbred BALB C - immunology Molecular Sequence Data Molecular weight Monoclonal antibodies monocotiledoneas monocotyledone monocotyledons peptide peptides Peptides - chemical synthesis peptidos Plants Plants - enzymology protected cultivation Protein Conformation Proteins purificacion purification reaccion de inmunoprecipitacion reaction d' immunoprecipitation Sequence Homology, Nucleic Acid serre Species Specificity Zea mays |
| title | Production of a monocot-specific monoclonal antibody against acetohydroxyacid synthase and its use in the purification and characterization of the enzyme |
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