Primary Structure of very Low Density Apolipoprotein C-II of Human Plasma
Apolipoprotein C-II (apoC-II), a protein constituent of very low density lipoproteins of human plasma and the activator protein of lipoprotein lipase, has been isolated and its amino acid sequence has been studied. The protein has 78 amino acid residues and is lacking cysteine, cystine, and histidin...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1977-05, Vol.74 (5), p.1942-1945 |
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| container_end_page | 1945 |
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| container_issue | 5 |
| container_start_page | 1942 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 74 |
| creator | Jackson, Richard L. Baker, H. Nordean Gilliam, Ellen B. Gotto, Antonio M. |
| description | Apolipoprotein C-II (apoC-II), a protein constituent of very low density lipoproteins of human plasma and the activator protein of lipoprotein lipase, has been isolated and its amino acid sequence has been studied. The protein has 78 amino acid residues and is lacking cysteine, cystine, and histidine. Chromatography on Bio-Gel P-30 in 25% formic acid of the cyanogen bromide digest of apoC-II yields three fragments designated as CNBr-I, -II, and -III. They contained 50, 19, and 9 residues, respectively. The alignment of the cyanogen bromide fragments has been established as CNBr-III-I-II by isolation and sequence of the tryptic peptides of the intact protein. The amino acid sequences of the tryptic and CNBr peptides were determined by conventional methods. With this information, it was possible to establish the complete amino acid sequence of apoC-II. |
| doi_str_mv | 10.1073/pnas.74.5.1942 |
| format | Article |
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Nordean ; Gilliam, Ellen B. ; Gotto, Antonio M.</creator><creatorcontrib>Jackson, Richard L. ; Baker, H. Nordean ; Gilliam, Ellen B. ; Gotto, Antonio M.</creatorcontrib><description>Apolipoprotein C-II (apoC-II), a protein constituent of very low density lipoproteins of human plasma and the activator protein of lipoprotein lipase, has been isolated and its amino acid sequence has been studied. The protein has 78 amino acid residues and is lacking cysteine, cystine, and histidine. Chromatography on Bio-Gel P-30 in 25% formic acid of the cyanogen bromide digest of apoC-II yields three fragments designated as CNBr-I, -II, and -III. They contained 50, 19, and 9 residues, respectively. The alignment of the cyanogen bromide fragments has been established as CNBr-III-I-II by isolation and sequence of the tryptic peptides of the intact protein. The amino acid sequences of the tryptic and CNBr peptides were determined by conventional methods. With this information, it was possible to establish the complete amino acid sequence of apoC-II.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.74.5.1942</identifier><identifier>PMID: 194244</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Amino acids ; Apolipoproteins - blood ; Apolipoproteins - isolation & purification ; Apoproteins ; Atherosclerosis ; Biochemistry ; Bromides ; Chromatography ; Cyanogen Bromide ; Humans ; Hydrolysis ; Lipids ; Lipoproteins ; Lipoproteins, VLDL - blood ; Plasma density ; Trypsin - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1977-05, Vol.74 (5), p.1942-1945</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3702-9d35fbd34b558b8fcca8b94783b58c7fe0a14c5b0aadde051031de1a7f2494063</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/74/5.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/67141$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/67141$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,724,777,781,800,882,27905,27906,53772,53774,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/194244$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jackson, Richard L.</creatorcontrib><creatorcontrib>Baker, H. Nordean</creatorcontrib><creatorcontrib>Gilliam, Ellen B.</creatorcontrib><creatorcontrib>Gotto, Antonio M.</creatorcontrib><title>Primary Structure of very Low Density Apolipoprotein C-II of Human Plasma</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Apolipoprotein C-II (apoC-II), a protein constituent of very low density lipoproteins of human plasma and the activator protein of lipoprotein lipase, has been isolated and its amino acid sequence has been studied. The protein has 78 amino acid residues and is lacking cysteine, cystine, and histidine. Chromatography on Bio-Gel P-30 in 25% formic acid of the cyanogen bromide digest of apoC-II yields three fragments designated as CNBr-I, -II, and -III. They contained 50, 19, and 9 residues, respectively. The alignment of the cyanogen bromide fragments has been established as CNBr-III-I-II by isolation and sequence of the tryptic peptides of the intact protein. The amino acid sequences of the tryptic and CNBr peptides were determined by conventional methods. With this information, it was possible to establish the complete amino acid sequence of apoC-II.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Apolipoproteins - blood</subject><subject>Apolipoproteins - isolation & purification</subject><subject>Apoproteins</subject><subject>Atherosclerosis</subject><subject>Biochemistry</subject><subject>Bromides</subject><subject>Chromatography</subject><subject>Cyanogen Bromide</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Lipids</subject><subject>Lipoproteins</subject><subject>Lipoproteins, VLDL - blood</subject><subject>Plasma density</subject><subject>Trypsin - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kDFP3DAYhi3UQq_A2gGBlKlbwufYPtsDA7pCOekkkIDZchyHBiVxsB0o_74JRw9YmCz5fR5_n1-EfmDIMHBy3Hc6ZJxmLMOS5ltohkHidE4lfEEzgJyngub0G_oewj0ASCZgB21PLKUztLzydav9c3Id_WDi4G3iquTRjjcr95T8sl2o43Ny2rum7l3vXbR1lyzS5XLiLoZWd8lVo0Or99DXSjfB7r-eu-j2_OxmcZGuLn8vF6er1BAOeSpLwqqiJLRgTBSiMkaLQlIuSMGE4ZUFjalhBWhdlhYYBoJLizWvciopzMkuOlm_2w9Fa0tju-h1o_r1P5TTtfqYdPUfdeceFSUYqBj9n6--dw-DDVG1dTC2aXRn3RCUIDLnAuQIZmvQeBeCt9VmBgY1Va-m6hWniqmpzlE4fL_ZG_7S9bvBk_Y_3OiqGpom2r9xBI8-A8f8YJ3fh-j8BphzTDH5B5jKoQk</recordid><startdate>19770501</startdate><enddate>19770501</enddate><creator>Jackson, Richard L.</creator><creator>Baker, H. Nordean</creator><creator>Gilliam, Ellen B.</creator><creator>Gotto, Antonio M.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19770501</creationdate><title>Primary Structure of very Low Density Apolipoprotein C-II of Human Plasma</title><author>Jackson, Richard L. ; Baker, H. Nordean ; Gilliam, Ellen B. ; Gotto, Antonio M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3702-9d35fbd34b558b8fcca8b94783b58c7fe0a14c5b0aadde051031de1a7f2494063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Apolipoproteins - blood</topic><topic>Apolipoproteins - isolation & purification</topic><topic>Apoproteins</topic><topic>Atherosclerosis</topic><topic>Biochemistry</topic><topic>Bromides</topic><topic>Chromatography</topic><topic>Cyanogen Bromide</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Lipids</topic><topic>Lipoproteins</topic><topic>Lipoproteins, VLDL - blood</topic><topic>Plasma density</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jackson, Richard L.</creatorcontrib><creatorcontrib>Baker, H. Nordean</creatorcontrib><creatorcontrib>Gilliam, Ellen B.</creatorcontrib><creatorcontrib>Gotto, Antonio M.</creatorcontrib><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><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>Jackson, Richard L.</au><au>Baker, H. Nordean</au><au>Gilliam, Ellen B.</au><au>Gotto, Antonio M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Primary Structure of very Low Density Apolipoprotein C-II of Human Plasma</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1977-05-01</date><risdate>1977</risdate><volume>74</volume><issue>5</issue><spage>1942</spage><epage>1945</epage><pages>1942-1945</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Apolipoprotein C-II (apoC-II), a protein constituent of very low density lipoproteins of human plasma and the activator protein of lipoprotein lipase, has been isolated and its amino acid sequence has been studied. The protein has 78 amino acid residues and is lacking cysteine, cystine, and histidine. Chromatography on Bio-Gel P-30 in 25% formic acid of the cyanogen bromide digest of apoC-II yields three fragments designated as CNBr-I, -II, and -III. They contained 50, 19, and 9 residues, respectively. The alignment of the cyanogen bromide fragments has been established as CNBr-III-I-II by isolation and sequence of the tryptic peptides of the intact protein. The amino acid sequences of the tryptic and CNBr peptides were determined by conventional methods. With this information, it was possible to establish the complete amino acid sequence of apoC-II.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>194244</pmid><doi>10.1073/pnas.74.5.1942</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1977-05, Vol.74 (5), p.1942-1945 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Amino acids Apolipoproteins - blood Apolipoproteins - isolation & purification Apoproteins Atherosclerosis Biochemistry Bromides Chromatography Cyanogen Bromide Humans Hydrolysis Lipids Lipoproteins Lipoproteins, VLDL - blood Plasma density Trypsin - metabolism |
| title | Primary Structure of very Low Density Apolipoprotein C-II of Human Plasma |
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