Resolution of pea legumin subunits by high-performance liquid chromatography
Pea legumin was dissociated into its component subunits by 6 m urea: these were subsequently fractionated by FPLC using a combination of Mono P, Mono Q, and Mono S columns. The resolution and speed of separation were greatly improved in comparison with previous fractionations. Twelve discrete fracti...
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| Veröffentlicht in: | Analytical biochemistry 1987, Vol.160 (1), p.202-210 |
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| container_title | Analytical biochemistry |
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| creator | Bacon, J.R. Lambert, N. Phalp, M. Plumb, G.W. Wright, D.J. |
| description | Pea legumin was dissociated into its component subunits by 6
m urea: these were subsequently fractionated by FPLC using a combination of Mono P, Mono Q, and Mono S columns. The resolution and speed of separation were greatly improved in comparison with previous fractionations. Twelve discrete fractions were obtained and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Six “normal” legumin subunits (
M
r 60,000) were identified as well as some “large” (
M
r 66,000) and “small” (
M
r 44,000) subunits. A few polypeptides of unknown origin were also observed. Four subunits were purified to homogeneity as adjudged by electrophoresis and HPLC and in sufficient yields to permit further studies. Anomalous electrophoretic behavior of the legumin subunits was also observed. |
| doi_str_mv | 10.1016/0003-2697(87)90631-2 |
| format | Article |
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m urea: these were subsequently fractionated by FPLC using a combination of Mono P, Mono Q, and Mono S columns. The resolution and speed of separation were greatly improved in comparison with previous fractionations. Twelve discrete fractions were obtained and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Six “normal” legumin subunits (
M
r 60,000) were identified as well as some “large” (
M
r 66,000) and “small” (
M
r 44,000) subunits. A few polypeptides of unknown origin were also observed. Four subunits were purified to homogeneity as adjudged by electrophoresis and HPLC and in sufficient yields to permit further studies. Anomalous electrophoretic behavior of the legumin subunits was also observed.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/0003-2697(87)90631-2</identifier><identifier>PMID: 3565752</identifier><identifier>CODEN: ANBCA2</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Chromatography, High Pressure Liquid - methods ; electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Fabaceae ; Fundamental and applied biological sciences. Psychology ; Holoproteins ; HPLC, proteins ; legumin ; Legumins ; Macromolecular Substances ; Molecular Weight ; Other proteins ; pea legumin ; Pisum sativum ; Plant Proteins ; Plant Proteins, Dietary ; Plants, Medicinal ; Proteins ; subunit structure</subject><ispartof>Analytical biochemistry, 1987, Vol.160 (1), p.202-210</ispartof><rights>1987</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-b72d371e0cb5be5b80f9eb40661e18964f7941ad42f269b9aadac9eedd39c62b3</citedby><cites>FETCH-LOGICAL-c463t-b72d371e0cb5be5b80f9eb40661e18964f7941ad42f269b9aadac9eedd39c62b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003269787906312$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7409273$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3565752$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bacon, J.R.</creatorcontrib><creatorcontrib>Lambert, N.</creatorcontrib><creatorcontrib>Phalp, M.</creatorcontrib><creatorcontrib>Plumb, G.W.</creatorcontrib><creatorcontrib>Wright, D.J.</creatorcontrib><title>Resolution of pea legumin subunits by high-performance liquid chromatography</title><title>Analytical biochemistry</title><addtitle>Anal Biochem</addtitle><description>Pea legumin was dissociated into its component subunits by 6
m urea: these were subsequently fractionated by FPLC using a combination of Mono P, Mono Q, and Mono S columns. The resolution and speed of separation were greatly improved in comparison with previous fractionations. Twelve discrete fractions were obtained and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Six “normal” legumin subunits (
M
r 60,000) were identified as well as some “large” (
M
r 66,000) and “small” (
M
r 44,000) subunits. A few polypeptides of unknown origin were also observed. Four subunits were purified to homogeneity as adjudged by electrophoresis and HPLC and in sufficient yields to permit further studies. Anomalous electrophoretic behavior of the legumin subunits was also observed.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chromatography, High Pressure Liquid - methods</subject><subject>electrophoresis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fabaceae</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Holoproteins</subject><subject>HPLC, proteins</subject><subject>legumin</subject><subject>Legumins</subject><subject>Macromolecular Substances</subject><subject>Molecular Weight</subject><subject>Other proteins</subject><subject>pea legumin</subject><subject>Pisum sativum</subject><subject>Plant Proteins</subject><subject>Plant Proteins, Dietary</subject><subject>Plants, Medicinal</subject><subject>Proteins</subject><subject>subunit structure</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3DAQhkVpSLdp_0EDPpTQHNyOLFmyLoEQ2rSwECjtWehjvKtgW45kB_bfx9td9tic5jDPO_PyEPKJwlcKVHwDAFZWQskvjbxWIBgtqzdkRUGJEhiot2R1Qt6R9zk_AlDKa3FOzlktallXK7L-jTl28xTiUMS2GNEUHW7mPgxFnu08hCkXdldsw2ZbjpjamHozOCy68DQHX7htir2Z4iaZcbv7QM5a02X8eJwX5O-P73_ufpbrh_tfd7fr0nHBptLKyjNJEZytLda2gVah5SAERdoowVupODWeV-3S3SpjvHEK0XumnKgsuyBXh7tjik8z5kn3ITvsOjNgnLOWkktQlL0KUr584w1fQH4AXYo5J2z1mEJv0k5T0Hvbeq9S71XqRup_tnW1xC6P92fboz-FjnqX_efj3mRnujYt7kI-YZKDquS-5s0Bw0Xac8Ckswu4aPYhoZu0j-H_PV4A_sqcCA</recordid><startdate>1987</startdate><enddate>1987</enddate><creator>Bacon, J.R.</creator><creator>Lambert, N.</creator><creator>Phalp, M.</creator><creator>Plumb, G.W.</creator><creator>Wright, D.J.</creator><general>Elsevier Inc</general><general>Elsevier</general><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>C1K</scope><scope>7X8</scope></search><sort><creationdate>1987</creationdate><title>Resolution of pea legumin subunits by high-performance liquid chromatography</title><author>Bacon, J.R. ; Lambert, N. ; Phalp, M. ; Plumb, G.W. ; Wright, D.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-b72d371e0cb5be5b80f9eb40661e18964f7941ad42f269b9aadac9eedd39c62b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chromatography, High Pressure Liquid - methods</topic><topic>electrophoresis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fabaceae</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Holoproteins</topic><topic>HPLC, proteins</topic><topic>legumin</topic><topic>Legumins</topic><topic>Macromolecular Substances</topic><topic>Molecular Weight</topic><topic>Other proteins</topic><topic>pea legumin</topic><topic>Pisum sativum</topic><topic>Plant Proteins</topic><topic>Plant Proteins, Dietary</topic><topic>Plants, Medicinal</topic><topic>Proteins</topic><topic>subunit structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bacon, J.R.</creatorcontrib><creatorcontrib>Lambert, N.</creatorcontrib><creatorcontrib>Phalp, M.</creatorcontrib><creatorcontrib>Plumb, G.W.</creatorcontrib><creatorcontrib>Wright, D.J.</creatorcontrib><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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bacon, J.R.</au><au>Lambert, N.</au><au>Phalp, M.</au><au>Plumb, G.W.</au><au>Wright, D.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Resolution of pea legumin subunits by high-performance liquid chromatography</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>1987</date><risdate>1987</risdate><volume>160</volume><issue>1</issue><spage>202</spage><epage>210</epage><pages>202-210</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><coden>ANBCA2</coden><abstract>Pea legumin was dissociated into its component subunits by 6
m urea: these were subsequently fractionated by FPLC using a combination of Mono P, Mono Q, and Mono S columns. The resolution and speed of separation were greatly improved in comparison with previous fractionations. Twelve discrete fractions were obtained and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Six “normal” legumin subunits (
M
r 60,000) were identified as well as some “large” (
M
r 66,000) and “small” (
M
r 44,000) subunits. A few polypeptides of unknown origin were also observed. Four subunits were purified to homogeneity as adjudged by electrophoresis and HPLC and in sufficient yields to permit further studies. Anomalous electrophoretic behavior of the legumin subunits was also observed.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3565752</pmid><doi>10.1016/0003-2697(87)90631-2</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Analytical biochemistry, 1987, Vol.160 (1), p.202-210 |
| issn | 0003-2697 1096-0309 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Chromatography, High Pressure Liquid - methods electrophoresis Electrophoresis, Polyacrylamide Gel Fabaceae Fundamental and applied biological sciences. Psychology Holoproteins HPLC, proteins legumin Legumins Macromolecular Substances Molecular Weight Other proteins pea legumin Pisum sativum Plant Proteins Plant Proteins, Dietary Plants, Medicinal Proteins subunit structure |
| title | Resolution of pea legumin subunits by high-performance liquid chromatography |
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