Purification, Ultrastructure, and Chemical Analysis of Alzheimer Disease Amyloid Plaque Core Protein
Isolation of Alzheimer disease amyloid plaque core protein (APCP) was carried out by repetitive NaDodSO4/EDTA/sucrose extractions and by Ficoll-400 density-gradient centrifugations. The enriched APCP-Ficoll interface was labeled with the fluorochrome thioflavin T and separated from the contaminating...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1986-04, Vol.83 (8), p.2662-2666 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2666 |
|---|---|
| container_issue | 8 |
| container_start_page | 2662 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 83 |
| creator | Roher, Alex Wolfe, David Palutke, Margarita KuKuruga, Debra |
| description | Isolation of Alzheimer disease amyloid plaque core protein (APCP) was carried out by repetitive NaDodSO4/EDTA/sucrose extractions and by Ficoll-400 density-gradient centrifugations. The enriched APCP-Ficoll interface was labeled with the fluorochrome thioflavin T and separated from the contaminating lipofuscin by fluorescence-activated cell sorting. Electron microscopy demonstrated that APCP is made of two different kinds of filaments measuring 5.5-6 nm and 10-12 nm, respectively, and of variable length. Purified APCP and lipofuscin were chemically modified by performic acid oxidation. The amino acid composition of APCP revealed a high content of glycine and valine (30%) and 1% cysteine. By contrast, the protein moiety of the copurified lipofuscin contained 16% cysteine. The amino acid composition of APCP did not resemble that of any known protein. |
| doi_str_mv | 10.1073/pnas.83.8.2662 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pasca</sourceid><recordid>TN_cdi_pascalfrancis_primary_8699148</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>27345</jstor_id><sourcerecordid>27345</sourcerecordid><originalsourceid>FETCH-LOGICAL-c485t-30ca363b36bedcb358e269bd68cf4d2bcdf532cdceb4d5f9dfd72fe147077d283</originalsourceid><addsrcrecordid>eNp9kTuP1DAUhS0EWoaFlgIJyQXaahMc24mdYovR8JRWYgq2thw_GK-ceLAdxPDr8WhG0dBQuTjfOfdeHwBeN6huECPv95NMNSc1r3HX4Sdg1aC-qTrao6dghRBmFaeYPgcvUnpECPUtR1fgitCWY0xXQG_n6KxTMrsw3cIHn6NMOc4qz9HcQjlpuNmZsQAerifpD8klGCxc-z8740YT4QeXjEwGrseDD07DrZc_ZwM3IRq4jSEbN70Ez6z0ybw6v9fg4dPH75sv1f23z1836_tKUd7miiAlSUcG0g1Gq4G03OCuH3THlaUaD0rblmCllRmobm2vrWbYmoYyxJjGnFyDu1Pufh7GEmGmco0X--hGGQ8iSCf-VSa3Ez_CL0EwIW1f_DdnfwzlhpTF6JIy3svJhDkJ1nHMOGoLWJ9AFUNK0dhlRoPEsRZxrEVwIrg41lIMby83W_BzD0V_d9ZlKl9to5yUSwvGu75vKL-IOcYv6sWYm__pws7eZ_M7F_DNCXxMOcSFxKwsRP4CR2O5pQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76827805</pqid></control><display><type>article</type><title>Purification, Ultrastructure, and Chemical Analysis of Alzheimer Disease Amyloid Plaque Core Protein</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Roher, Alex ; Wolfe, David ; Palutke, Margarita ; KuKuruga, Debra</creator><creatorcontrib>Roher, Alex ; Wolfe, David ; Palutke, Margarita ; KuKuruga, Debra</creatorcontrib><description>Isolation of Alzheimer disease amyloid plaque core protein (APCP) was carried out by repetitive NaDodSO4/EDTA/sucrose extractions and by Ficoll-400 density-gradient centrifugations. The enriched APCP-Ficoll interface was labeled with the fluorochrome thioflavin T and separated from the contaminating lipofuscin by fluorescence-activated cell sorting. Electron microscopy demonstrated that APCP is made of two different kinds of filaments measuring 5.5-6 nm and 10-12 nm, respectively, and of variable length. Purified APCP and lipofuscin were chemically modified by performic acid oxidation. The amino acid composition of APCP revealed a high content of glycine and valine (30%) and 1% cysteine. By contrast, the protein moiety of the copurified lipofuscin contained 16% cysteine. The amino acid composition of APCP did not resemble that of any known protein.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.83.8.2662</identifier><identifier>PMID: 3458224</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Alzheimer Disease - metabolism ; Alzheimers disease ; Amino acids ; Amino Acids - analysis ; Amyloid - isolation & purification ; Amyloid - metabolism ; Amyloid plaque ; Amyloids ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Brain Chemistry ; Centrifugation ; Chemical composition ; Electron microscopy ; Flow Cytometry ; Fundamental and applied biological sciences. Psychology ; Humans ; Lipofuscin - isolation & purification ; Microscopy, Electron ; Miscellaneous ; Nerve Tissue Proteins - isolation & purification ; Nerve Tissue Proteins - metabolism ; Neurofibrillary tangles ; Neurons ; Oxidation ; Proteins ; Solubility</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1986-04, Vol.83 (8), p.2662-2666</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c485t-30ca363b36bedcb358e269bd68cf4d2bcdf532cdceb4d5f9dfd72fe147077d283</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/83/8.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/27345$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/27345$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8699148$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3458224$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roher, Alex</creatorcontrib><creatorcontrib>Wolfe, David</creatorcontrib><creatorcontrib>Palutke, Margarita</creatorcontrib><creatorcontrib>KuKuruga, Debra</creatorcontrib><title>Purification, Ultrastructure, and Chemical Analysis of Alzheimer Disease Amyloid Plaque Core Protein</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Isolation of Alzheimer disease amyloid plaque core protein (APCP) was carried out by repetitive NaDodSO4/EDTA/sucrose extractions and by Ficoll-400 density-gradient centrifugations. The enriched APCP-Ficoll interface was labeled with the fluorochrome thioflavin T and separated from the contaminating lipofuscin by fluorescence-activated cell sorting. Electron microscopy demonstrated that APCP is made of two different kinds of filaments measuring 5.5-6 nm and 10-12 nm, respectively, and of variable length. Purified APCP and lipofuscin were chemically modified by performic acid oxidation. The amino acid composition of APCP revealed a high content of glycine and valine (30%) and 1% cysteine. By contrast, the protein moiety of the copurified lipofuscin contained 16% cysteine. The amino acid composition of APCP did not resemble that of any known protein.</description><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimers disease</subject><subject>Amino acids</subject><subject>Amino Acids - analysis</subject><subject>Amyloid - isolation & purification</subject><subject>Amyloid - metabolism</subject><subject>Amyloid plaque</subject><subject>Amyloids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Brain Chemistry</subject><subject>Centrifugation</subject><subject>Chemical composition</subject><subject>Electron microscopy</subject><subject>Flow Cytometry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Lipofuscin - isolation & purification</subject><subject>Microscopy, Electron</subject><subject>Miscellaneous</subject><subject>Nerve Tissue Proteins - isolation & purification</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurofibrillary tangles</subject><subject>Neurons</subject><subject>Oxidation</subject><subject>Proteins</subject><subject>Solubility</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kTuP1DAUhS0EWoaFlgIJyQXaahMc24mdYovR8JRWYgq2thw_GK-ceLAdxPDr8WhG0dBQuTjfOfdeHwBeN6huECPv95NMNSc1r3HX4Sdg1aC-qTrao6dghRBmFaeYPgcvUnpECPUtR1fgitCWY0xXQG_n6KxTMrsw3cIHn6NMOc4qz9HcQjlpuNmZsQAerifpD8klGCxc-z8740YT4QeXjEwGrseDD07DrZc_ZwM3IRq4jSEbN70Ez6z0ybw6v9fg4dPH75sv1f23z1836_tKUd7miiAlSUcG0g1Gq4G03OCuH3THlaUaD0rblmCllRmobm2vrWbYmoYyxJjGnFyDu1Pufh7GEmGmco0X--hGGQ8iSCf-VSa3Ez_CL0EwIW1f_DdnfwzlhpTF6JIy3svJhDkJ1nHMOGoLWJ9AFUNK0dhlRoPEsRZxrEVwIrg41lIMby83W_BzD0V_d9ZlKl9to5yUSwvGu75vKL-IOcYv6sWYm__pws7eZ_M7F_DNCXxMOcSFxKwsRP4CR2O5pQ</recordid><startdate>19860401</startdate><enddate>19860401</enddate><creator>Roher, Alex</creator><creator>Wolfe, David</creator><creator>Palutke, Margarita</creator><creator>KuKuruga, Debra</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19860401</creationdate><title>Purification, Ultrastructure, and Chemical Analysis of Alzheimer Disease Amyloid Plaque Core Protein</title><author>Roher, Alex ; Wolfe, David ; Palutke, Margarita ; KuKuruga, Debra</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c485t-30ca363b36bedcb358e269bd68cf4d2bcdf532cdceb4d5f9dfd72fe147077d283</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimers disease</topic><topic>Amino acids</topic><topic>Amino Acids - analysis</topic><topic>Amyloid - isolation & purification</topic><topic>Amyloid - metabolism</topic><topic>Amyloid plaque</topic><topic>Amyloids</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Brain Chemistry</topic><topic>Centrifugation</topic><topic>Chemical composition</topic><topic>Electron microscopy</topic><topic>Flow Cytometry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Lipofuscin - isolation & purification</topic><topic>Microscopy, Electron</topic><topic>Miscellaneous</topic><topic>Nerve Tissue Proteins - isolation & purification</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurofibrillary tangles</topic><topic>Neurons</topic><topic>Oxidation</topic><topic>Proteins</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roher, Alex</creatorcontrib><creatorcontrib>Wolfe, David</creatorcontrib><creatorcontrib>Palutke, Margarita</creatorcontrib><creatorcontrib>KuKuruga, Debra</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>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>Roher, Alex</au><au>Wolfe, David</au><au>Palutke, Margarita</au><au>KuKuruga, Debra</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, Ultrastructure, and Chemical Analysis of Alzheimer Disease Amyloid Plaque Core Protein</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1986-04-01</date><risdate>1986</risdate><volume>83</volume><issue>8</issue><spage>2662</spage><epage>2666</epage><pages>2662-2666</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Isolation of Alzheimer disease amyloid plaque core protein (APCP) was carried out by repetitive NaDodSO4/EDTA/sucrose extractions and by Ficoll-400 density-gradient centrifugations. The enriched APCP-Ficoll interface was labeled with the fluorochrome thioflavin T and separated from the contaminating lipofuscin by fluorescence-activated cell sorting. Electron microscopy demonstrated that APCP is made of two different kinds of filaments measuring 5.5-6 nm and 10-12 nm, respectively, and of variable length. Purified APCP and lipofuscin were chemically modified by performic acid oxidation. The amino acid composition of APCP revealed a high content of glycine and valine (30%) and 1% cysteine. By contrast, the protein moiety of the copurified lipofuscin contained 16% cysteine. The amino acid composition of APCP did not resemble that of any known protein.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3458224</pmid><doi>10.1073/pnas.83.8.2662</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1986-04, Vol.83 (8), p.2662-2666 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_8699148 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Alzheimer Disease - metabolism Alzheimers disease Amino acids Amino Acids - analysis Amyloid - isolation & purification Amyloid - metabolism Amyloid plaque Amyloids Analytical, structural and metabolic biochemistry Biological and medical sciences Brain Chemistry Centrifugation Chemical composition Electron microscopy Flow Cytometry Fundamental and applied biological sciences. Psychology Humans Lipofuscin - isolation & purification Microscopy, Electron Miscellaneous Nerve Tissue Proteins - isolation & purification Nerve Tissue Proteins - metabolism Neurofibrillary tangles Neurons Oxidation Proteins Solubility |
| title | Purification, Ultrastructure, and Chemical Analysis of Alzheimer Disease Amyloid Plaque Core Protein |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T15%3A44%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification,%20Ultrastructure,%20and%20Chemical%20Analysis%20of%20Alzheimer%20Disease%20Amyloid%20Plaque%20Core%20Protein&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Roher,%20Alex&rft.date=1986-04-01&rft.volume=83&rft.issue=8&rft.spage=2662&rft.epage=2666&rft.pages=2662-2666&rft.issn=0027-8424&rft.eissn=1091-6490&rft.coden=PNASA6&rft_id=info:doi/10.1073/pnas.83.8.2662&rft_dat=%3Cjstor_pasca%3E27345%3C/jstor_pasca%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=76827805&rft_id=info:pmid/3458224&rft_jstor_id=27345&rfr_iscdi=true |