Starch in fungi IV. The lipoprotein amylose-precipitating factor
The amylose precipitating factor from Neurospora is a lipoprotein of 53,800 mw. The lipid component, which is responsible for the amylose precipitating activity, is mainly polar lipid and constitutes 14.5% of the lipoprotein molecule. The binding of amylose to the amylose precipitating factor possib...
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Veröffentlicht in: | Biochemical and biophysical research communications 1980-04, Vol.93 (4), p.1204-1209 |
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description | The amylose precipitating factor from
Neurospora is a lipoprotein of 53,800 mw. The lipid component, which is responsible for the amylose precipitating activity, is mainly polar lipid and constitutes 14.5% of the lipoprotein molecule. The binding of amylose to the amylose precipitating factor possibly results in the conversion of the amylose molecule from a random coil to an interrupted helix configuration. |
doi_str_mv | 10.1016/0006-291X(80)90617-8 |
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Neurospora is a lipoprotein of 53,800 mw. The lipid component, which is responsible for the amylose precipitating activity, is mainly polar lipid and constitutes 14.5% of the lipoprotein molecule. The binding of amylose to the amylose precipitating factor possibly results in the conversion of the amylose molecule from a random coil to an interrupted helix configuration.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(80)90617-8</identifier><identifier>PMID: 6446910</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amylose - metabolism ; Apolipoproteins - isolation & purification ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; Chemical Precipitation ; Fungal Proteins - isolation & purification ; Lipoproteins - isolation & purification ; Molecular Weight ; Neurospora - analysis ; Neurospora crassa - analysis ; Neurospora crassa - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1980-04, Vol.93 (4), p.1204-1209</ispartof><rights>1980</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c272t-cd66ebf8d6750861697991ac82b8a53f9c0b641c9551a1c2b67d47dd93e14fbe3</citedby><cites>FETCH-LOGICAL-c272t-cd66ebf8d6750861697991ac82b8a53f9c0b641c9551a1c2b67d47dd93e14fbe3</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(80)90617-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6446910$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McCracken, Derek A.</creatorcontrib><creatorcontrib>Rutherford, William M.</creatorcontrib><title>Starch in fungi IV. The lipoprotein amylose-precipitating factor</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The amylose precipitating factor from
Neurospora is a lipoprotein of 53,800 mw. The lipid component, which is responsible for the amylose precipitating activity, is mainly polar lipid and constitutes 14.5% of the lipoprotein molecule. The binding of amylose to the amylose precipitating factor possibly results in the conversion of the amylose molecule from a random coil to an interrupted helix configuration.</description><subject>Amylose - metabolism</subject><subject>Apolipoproteins - isolation & purification</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>Chemical Precipitation</subject><subject>Fungal Proteins - isolation & purification</subject><subject>Lipoproteins - isolation & purification</subject><subject>Molecular Weight</subject><subject>Neurospora - analysis</subject><subject>Neurospora crassa - analysis</subject><subject>Neurospora crassa - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1Lw0AQhhdRaq3-A4WcRA-pM2my2b2IUvwoFDxYxduy2UzalTSJu4nQf29qi0dPc3g_ZuZh7BxhjID8BgB4GEn8uBJwLYFjGooDNkSQEEYI8SEb_lmO2Yn3nwCIMZcDNuBxPxGG7O611c6sAlsFRVctbTB7HweLFQWlberG1S31il5vytpT2DgytrGtbm21DApt2tqdsqNCl57O9nPE3h4fFtPncP7yNJvez0MTpVEbmpxzygqR8zQBwZHLVErURkSZ0MmkkAYyHqORSYIaTZTxNI_TPJcTwrjIaDJil7ve_qivjnyr1tYbKktdUd15lSYoklRMemO8MxpXe--oUI2za-02CkFtwaktFbWlogSoX3BK9LGLfX-XrSn_C-1J9frtTqf-yW9LTnljqTKU255Kq_La_r_gB89rfIU</recordid><startdate>19800429</startdate><enddate>19800429</enddate><creator>McCracken, Derek A.</creator><creator>Rutherford, William M.</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>19800429</creationdate><title>Starch in fungi IV. The lipoprotein amylose-precipitating factor</title><author>McCracken, Derek A. ; Rutherford, William M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c272t-cd66ebf8d6750861697991ac82b8a53f9c0b641c9551a1c2b67d47dd93e14fbe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Amylose - metabolism</topic><topic>Apolipoproteins - isolation & purification</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>Chemical Precipitation</topic><topic>Fungal Proteins - isolation & purification</topic><topic>Lipoproteins - isolation & purification</topic><topic>Molecular Weight</topic><topic>Neurospora - analysis</topic><topic>Neurospora crassa - analysis</topic><topic>Neurospora crassa - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McCracken, Derek A.</creatorcontrib><creatorcontrib>Rutherford, William 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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McCracken, Derek A.</au><au>Rutherford, William M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Starch in fungi IV. The lipoprotein amylose-precipitating factor</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1980-04-29</date><risdate>1980</risdate><volume>93</volume><issue>4</issue><spage>1204</spage><epage>1209</epage><pages>1204-1209</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The amylose precipitating factor from
Neurospora is a lipoprotein of 53,800 mw. The lipid component, which is responsible for the amylose precipitating activity, is mainly polar lipid and constitutes 14.5% of the lipoprotein molecule. The binding of amylose to the amylose precipitating factor possibly results in the conversion of the amylose molecule from a random coil to an interrupted helix configuration.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6446910</pmid><doi>10.1016/0006-291X(80)90617-8</doi><tpages>6</tpages></addata></record> |
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subjects | Amylose - metabolism Apolipoproteins - isolation & purification Carrier Proteins - isolation & purification Carrier Proteins - metabolism Chemical Precipitation Fungal Proteins - isolation & purification Lipoproteins - isolation & purification Molecular Weight Neurospora - analysis Neurospora crassa - analysis Neurospora crassa - metabolism |
title | Starch in fungi IV. The lipoprotein amylose-precipitating factor |
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