The structure and properties of human beta-lipoprotein and beta-apoprotein
Little is known about the structure of the protein of serum beta-lipoprotein owing to the insolubility of the delipidated product (beta-apoprotein). Attempts have been made to solubilize the apoprotein (Granda and Scanu, 1966) or a chemical derivative of the apoprotein ( Gotto et al., 1968a, b, c; S...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1968-06, Vol.31 (5), p.699-705 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Gotto, A.M. Levy, R.I. Rosenthal, A.S. Birnbaumer, M.E. Fredrickson, D.S. |
| description | Little is known about the structure of the protein of serum beta-lipoprotein owing to the insolubility of the delipidated product (beta-apoprotein). Attempts have been made to solubilize the apoprotein
(Granda and Scanu, 1966) or a chemical derivative of the apoprotein (
Gotto et al., 1968a, b, c;
Scanu et al., 1967;
Shore and Shore, 1967). This communication describes the preparation of beta-apoprotein by solubilization with sodium decyl sulfate. The apoprotein closely resembles the parent lipoprotein in immunological properties and structural conformation. The circular dichroism and infrared spectrum of beta-lipoprotein indicate a significant amount of pleated sheet, anti-parallel chain (APC) β-structure. This is also true for the apoprotein, except that the molar ellipticity at 216 mμ ([θ′]
216) is reduced by about 25%. The apoprotein has a fibrillar appearance when viewed with the electron microscope by the technique of negative staining. |
| doi_str_mv | 10.1016/0006-291X(68)90618-9 |
| format | Article |
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(Granda and Scanu, 1966) or a chemical derivative of the apoprotein (
Gotto et al., 1968a, b, c;
Scanu et al., 1967;
Shore and Shore, 1967). This communication describes the preparation of beta-apoprotein by solubilization with sodium decyl sulfate. The apoprotein closely resembles the parent lipoprotein in immunological properties and structural conformation. The circular dichroism and infrared spectrum of beta-lipoprotein indicate a significant amount of pleated sheet, anti-parallel chain (APC) β-structure. This is also true for the apoprotein, except that the molar ellipticity at 216 mμ ([θ′]
216) is reduced by about 25%. The apoprotein has a fibrillar appearance when viewed with the electron microscope by the technique of negative staining.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(68)90618-9</identifier><identifier>PMID: 4969860</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Blood Proteins - analysis ; Detergents ; Humans ; Immunodiffusion ; Immunoelectrophoresis ; Lipoproteins - blood ; Microscopy, Electron ; Optical Rotatory Dispersion ; Spectrophotometry</subject><ispartof>Biochemical and biophysical research communications, 1968-06, Vol.31 (5), p.699-705</ispartof><rights>1968</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-ba21ef572c3c616f276b08af93b70c8b54ed0b735d0e1f11d79ebb2989a562f93</citedby><cites>FETCH-LOGICAL-c357t-ba21ef572c3c616f276b08af93b70c8b54ed0b735d0e1f11d79ebb2989a562f93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(68)90618-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4969860$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gotto, A.M.</creatorcontrib><creatorcontrib>Levy, R.I.</creatorcontrib><creatorcontrib>Rosenthal, A.S.</creatorcontrib><creatorcontrib>Birnbaumer, M.E.</creatorcontrib><creatorcontrib>Fredrickson, D.S.</creatorcontrib><title>The structure and properties of human beta-lipoprotein and beta-apoprotein</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Little is known about the structure of the protein of serum beta-lipoprotein owing to the insolubility of the delipidated product (beta-apoprotein). Attempts have been made to solubilize the apoprotein
(Granda and Scanu, 1966) or a chemical derivative of the apoprotein (
Gotto et al., 1968a, b, c;
Scanu et al., 1967;
Shore and Shore, 1967). This communication describes the preparation of beta-apoprotein by solubilization with sodium decyl sulfate. The apoprotein closely resembles the parent lipoprotein in immunological properties and structural conformation. The circular dichroism and infrared spectrum of beta-lipoprotein indicate a significant amount of pleated sheet, anti-parallel chain (APC) β-structure. This is also true for the apoprotein, except that the molar ellipticity at 216 mμ ([θ′]
216) is reduced by about 25%. The apoprotein has a fibrillar appearance when viewed with the electron microscope by the technique of negative staining.</description><subject>Blood Proteins - analysis</subject><subject>Detergents</subject><subject>Humans</subject><subject>Immunodiffusion</subject><subject>Immunoelectrophoresis</subject><subject>Lipoproteins - blood</subject><subject>Microscopy, Electron</subject><subject>Optical Rotatory Dispersion</subject><subject>Spectrophotometry</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1968</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMo67r6DxR6Ej1UZ_qRNhdBFj9Z8LKCt5CkU4z0y6QV_Pe2u8sePQXmffIO8zB2jnCDgPwWAHgYCfy44vm1AI55KA7YHEFAGCEkh2y-R47ZifdfAIgJFzM2SwQXOYc5e11_UuB7N5h-cBSopgg613bkeks-aMvgc6hVE2jqVVjZrh3DnmyzATdDtZ-dsqNSVZ7Odu-CvT8-rJfP4ert6WV5vwpNnGZ9qFWEVKZZZGLDkZdRxjXkqhSxzsDkOk2oAJ3FaQGEJWKRCdI6ErlQKY9GbMEut73j3u-BfC9r6w1VlWqoHbzME4Eo0ngEky1oXOu9o1J2ztbK_UoEOSmUkx85-ZE8lxuFcuq_2PUPuqZi_2nnbMzvtjmNR_5YctIbS42hwjoyvSxa-_-CP9lWgSQ</recordid><startdate>19680610</startdate><enddate>19680610</enddate><creator>Gotto, A.M.</creator><creator>Levy, R.I.</creator><creator>Rosenthal, A.S.</creator><creator>Birnbaumer, M.E.</creator><creator>Fredrickson, D.S.</creator><general>Elsevier Inc</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></search><sort><creationdate>19680610</creationdate><title>The structure and properties of human beta-lipoprotein and beta-apoprotein</title><author>Gotto, A.M. ; Levy, R.I. ; Rosenthal, A.S. ; Birnbaumer, M.E. ; Fredrickson, D.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-ba21ef572c3c616f276b08af93b70c8b54ed0b735d0e1f11d79ebb2989a562f93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1968</creationdate><topic>Blood Proteins - analysis</topic><topic>Detergents</topic><topic>Humans</topic><topic>Immunodiffusion</topic><topic>Immunoelectrophoresis</topic><topic>Lipoproteins - blood</topic><topic>Microscopy, Electron</topic><topic>Optical Rotatory Dispersion</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gotto, A.M.</creatorcontrib><creatorcontrib>Levy, R.I.</creatorcontrib><creatorcontrib>Rosenthal, A.S.</creatorcontrib><creatorcontrib>Birnbaumer, M.E.</creatorcontrib><creatorcontrib>Fredrickson, D.S.</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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gotto, A.M.</au><au>Levy, R.I.</au><au>Rosenthal, A.S.</au><au>Birnbaumer, M.E.</au><au>Fredrickson, D.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The structure and properties of human beta-lipoprotein and beta-apoprotein</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1968-06-10</date><risdate>1968</risdate><volume>31</volume><issue>5</issue><spage>699</spage><epage>705</epage><pages>699-705</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Little is known about the structure of the protein of serum beta-lipoprotein owing to the insolubility of the delipidated product (beta-apoprotein). Attempts have been made to solubilize the apoprotein
(Granda and Scanu, 1966) or a chemical derivative of the apoprotein (
Gotto et al., 1968a, b, c;
Scanu et al., 1967;
Shore and Shore, 1967). This communication describes the preparation of beta-apoprotein by solubilization with sodium decyl sulfate. The apoprotein closely resembles the parent lipoprotein in immunological properties and structural conformation. The circular dichroism and infrared spectrum of beta-lipoprotein indicate a significant amount of pleated sheet, anti-parallel chain (APC) β-structure. This is also true for the apoprotein, except that the molar ellipticity at 216 mμ ([θ′]
216) is reduced by about 25%. The apoprotein has a fibrillar appearance when viewed with the electron microscope by the technique of negative staining.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4969860</pmid><doi>10.1016/0006-291X(68)90618-9</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1968-06, Vol.31 (5), p.699-705 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_84911953 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Blood Proteins - analysis Detergents Humans Immunodiffusion Immunoelectrophoresis Lipoproteins - blood Microscopy, Electron Optical Rotatory Dispersion Spectrophotometry |
| title | The structure and properties of human beta-lipoprotein and beta-apoprotein |
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