Molecular Cloning of 11S Globulin and 2S Albumin, the Two Major Seed Storage Proteins in Sesame
Insoluble 11S globulin and soluble 2S albumin, conventionally termed α-globulin and β-globulin, are the two major storage proteins and constitute 80−90% of total seed proteins in sesame. Two full-length cDNA clones were sequenced and deduced to encode sesame 11S globulin and 2S albumin precursors, r...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 1999-12, Vol.47 (12), p.4932-4938 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Tai, Sorgan S. K Wu, Lawrence S. H Chen, Emily C. F Tzen, Jason T. C |
| description | Insoluble 11S globulin and soluble 2S albumin, conventionally termed α-globulin and β-globulin, are the two major storage proteins and constitute 80−90% of total seed proteins in sesame. Two full-length cDNA clones were sequenced and deduced to encode sesame 11S globulin and 2S albumin precursors, respectively. Deduced amino acid composition reveals that 2S albumin, but not 11S globulin, is a sulfur-rich protein. Three abundant polypeptides of 50−60 kDa were resolved on SDS−PAGE when seed-purified 11S globulin was prepared in nonreducing conditions. Immunological analysis suggests that these three polypeptides are encoded by homologous genes. Immunodetection on the overexpressed protein of the 11S globulin clone in Escherichia coli indicates that this clone encodes the precursor protein of one of the three purified 11S globulin polypeptides. Keywords: 11S globulin; 2S albumin; seed; sesame; sulfur-rich protein |
| doi_str_mv | 10.1021/jf990366z |
| format | Article |
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Immunodetection on the overexpressed protein of the 11S globulin clone in Escherichia coli indicates that this clone encodes the precursor protein of one of the three purified 11S globulin polypeptides. Keywords: 11S globulin; 2S albumin; seed; sesame; sulfur-rich protein</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf990366z</identifier><identifier>PMID: 10606554</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Agronomy. Soil science and plant productions ; Amino Acid Sequence ; Biological and medical sciences ; Blotting, Western ; Chemical constitution ; Cloning, Molecular ; Economic plant physiology ; Electrophoresis, Polyacrylamide Gel ; Food industries ; Food Preservation ; Fruit and vegetable industries ; Fundamental and applied biological sciences. 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K</creatorcontrib><creatorcontrib>Wu, Lawrence S. H</creatorcontrib><creatorcontrib>Chen, Emily C. F</creatorcontrib><creatorcontrib>Tzen, Jason T. C</creatorcontrib><title>Molecular Cloning of 11S Globulin and 2S Albumin, the Two Major Seed Storage Proteins in Sesame</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Insoluble 11S globulin and soluble 2S albumin, conventionally termed α-globulin and β-globulin, are the two major storage proteins and constitute 80−90% of total seed proteins in sesame. Two full-length cDNA clones were sequenced and deduced to encode sesame 11S globulin and 2S albumin precursors, respectively. Deduced amino acid composition reveals that 2S albumin, but not 11S globulin, is a sulfur-rich protein. Three abundant polypeptides of 50−60 kDa were resolved on SDS−PAGE when seed-purified 11S globulin was prepared in nonreducing conditions. Immunological analysis suggests that these three polypeptides are encoded by homologous genes. Immunodetection on the overexpressed protein of the 11S globulin clone in Escherichia coli indicates that this clone encodes the precursor protein of one of the three purified 11S globulin polypeptides. Keywords: 11S globulin; 2S albumin; seed; sesame; sulfur-rich protein</description><subject>Agronomy. Soil science and plant productions</subject><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Chemical constitution</subject><subject>Cloning, Molecular</subject><subject>Economic plant physiology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Food industries</subject><subject>Food Preservation</subject><subject>Fruit and vegetable industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Library</subject><subject>Globulins - chemistry</subject><subject>Globulins - genetics</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Seeds - chemistry</subject><subject>Seeds - genetics</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0MFu1DAQBmALgei2cOAFkA-0EhKBcRLbybFaoK1oxUpZBDdr4kxKFicudiJanp6grFoOnObwfzMa_Yy9EPBWQCre7dqyhEyp34_YSsgUEilE8ZitYA6TQipxwA5j3AFAITU8ZQcCFCgp8xUzV96RnRwGvnZ-6IZr7lsuRMXPnK8n1w0ch4anFT919dR3wxs-fie-_eX5Fe584BVRw6vRB7wmvgl-pG6IfF6rKGJPz9iTFl2k5_t5xL58_LBdnyeXn88u1qeXCeZ5PiaYQU6o80ajRE1QSmsttIWtZWMLrKlImzJtSctaSVEUjVUibwhs2ijItc6O2Mly9yb4nxPF0fRdtOQcDuSnaFSZaShVNsPXC7TBxxioNTeh6zHcGQHmb5vmvs3Zvtwfneqemn_kUt8MXu0BRouuDTjYLj64NFdCq5klC-viSLf3MYYfRulMS7PdVCb79B42X7-V5nz2x4tHG83OT2GYq_vPf38AvBmWQg</recordid><startdate>19991201</startdate><enddate>19991201</enddate><creator>Tai, Sorgan S. 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Soil science and plant productions</topic><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Chemical constitution</topic><topic>Cloning, Molecular</topic><topic>Economic plant physiology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Food industries</topic><topic>Food Preservation</topic><topic>Fruit and vegetable industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Library</topic><topic>Globulins - chemistry</topic><topic>Globulins - genetics</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Seeds - chemistry</topic><topic>Seeds - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tai, Sorgan S. K</creatorcontrib><creatorcontrib>Wu, Lawrence S. H</creatorcontrib><creatorcontrib>Chen, Emily C. F</creatorcontrib><creatorcontrib>Tzen, Jason T. C</creatorcontrib><collection>Istex</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>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tai, Sorgan S. K</au><au>Wu, Lawrence S. H</au><au>Chen, Emily C. F</au><au>Tzen, Jason T. C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Cloning of 11S Globulin and 2S Albumin, the Two Major Seed Storage Proteins in Sesame</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1999-12-01</date><risdate>1999</risdate><volume>47</volume><issue>12</issue><spage>4932</spage><epage>4938</epage><pages>4932-4938</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Insoluble 11S globulin and soluble 2S albumin, conventionally termed α-globulin and β-globulin, are the two major storage proteins and constitute 80−90% of total seed proteins in sesame. Two full-length cDNA clones were sequenced and deduced to encode sesame 11S globulin and 2S albumin precursors, respectively. Deduced amino acid composition reveals that 2S albumin, but not 11S globulin, is a sulfur-rich protein. Three abundant polypeptides of 50−60 kDa were resolved on SDS−PAGE when seed-purified 11S globulin was prepared in nonreducing conditions. Immunological analysis suggests that these three polypeptides are encoded by homologous genes. Immunodetection on the overexpressed protein of the 11S globulin clone in Escherichia coli indicates that this clone encodes the precursor protein of one of the three purified 11S globulin polypeptides. Keywords: 11S globulin; 2S albumin; seed; sesame; sulfur-rich protein</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>10606554</pmid><doi>10.1021/jf990366z</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 1999-12, Vol.47 (12), p.4932-4938 |
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| source | ACS Publications; MEDLINE |
| subjects | Agronomy. Soil science and plant productions Amino Acid Sequence Biological and medical sciences Blotting, Western Chemical constitution Cloning, Molecular Economic plant physiology Electrophoresis, Polyacrylamide Gel Food industries Food Preservation Fruit and vegetable industries Fundamental and applied biological sciences. Psychology Gene Library Globulins - chemistry Globulins - genetics Humans Molecular Sequence Data Plant Proteins - chemistry Plant Proteins - genetics Seeds - chemistry Seeds - genetics |
| title | Molecular Cloning of 11S Globulin and 2S Albumin, the Two Major Seed Storage Proteins in Sesame |
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