Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change
Apolipophorin-III (apoLp-III), a hemolymph protein of Manduca sexta, can reversibly associate with the surface of lipoprotein particles. In order to examine the lipid-associated form of apoLp-III, the present studies investigate the structure and properties of apoLp-III complexes with dimyristoylpho...
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Veröffentlicht in: | The Journal of biological chemistry 1994-02, Vol.269 (6), p.4605-4612 |
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description | Apolipophorin-III (apoLp-III), a hemolymph protein of Manduca sexta, can reversibly associate with the surface of lipoprotein particles. In order to examine the lipid-associated form of apoLp-III, the present studies investigate the structure and properties of apoLp-III complexes with dimyristoylphosphatidylcholine (DMPC). Association of apoLp-III with DMPC vesicles results in the formation of uniform discs with an average diameter and width of 18.5 +/- 2.0 nm and 4.8 +/- 0.8 nm, respectively, as determined by electron microscopy. ApoLp-III-DMPC complexes analyzed by pore-limiting native gradient PAGE demonstrated that a single major species of complex was formed within a wide range of lipid to protein molar ratios (DMPC:apoLP-III; 13:1 to 360:1). Flotation equilibrium experiments, conducted in an analytical ultracentrifuge, confirmed that only one species of ApoLp-III-DMPC complex was formed at an initial lipid to protein molar ratio of 67:1, with an apparent molecular mass of 642,000. Complexes cross-linked with dimethyl suberimidate indicate that there are a maximum of 6 apoLp-III molecules per disc. Circular dichroism experiments revealed that apoLp-III becomes essentially completely alpha-helical on formation of apoLp-III-DMPC complexes. Compared to apoLp-III in the lipid-free state, apoLp-III-DMPC complexes were relatively resistant to denaturation by guanidine HCl, displaying denaturation transitions with midpoints at 2.2 and 3.7 m guanidine HCl, respectively. The fluorescence excitation and emission spectra of ApoLp-III-DMPC complexes demonstrate a large enhancement of tyrosine fluorescence as compared to the lipid-free state, suggesting that a conformational change occurs when apoLp-III associates with a lipid surface. Denaturation of apoLp-III in the complex by guanidine HCl resulted in a tyrosine fluorescence level similar to that of lipid-free apoLp-III in the presence of guanidine HCl |
doi_str_mv | 10.1016/S0021-9258(17)41819-9 |
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Evidence for a conformational change</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Wientzek, M ; Kay, C.M ; Oikawa, K ; Ryan, R.O</creator><creatorcontrib>Wientzek, M ; Kay, C.M ; Oikawa, K ; Ryan, R.O</creatorcontrib><description>Apolipophorin-III (apoLp-III), a hemolymph protein of Manduca sexta, can reversibly associate with the surface of lipoprotein particles. In order to examine the lipid-associated form of apoLp-III, the present studies investigate the structure and properties of apoLp-III complexes with dimyristoylphosphatidylcholine (DMPC). Association of apoLp-III with DMPC vesicles results in the formation of uniform discs with an average diameter and width of 18.5 +/- 2.0 nm and 4.8 +/- 0.8 nm, respectively, as determined by electron microscopy. ApoLp-III-DMPC complexes analyzed by pore-limiting native gradient PAGE demonstrated that a single major species of complex was formed within a wide range of lipid to protein molar ratios (DMPC:apoLP-III; 13:1 to 360:1). Flotation equilibrium experiments, conducted in an analytical ultracentrifuge, confirmed that only one species of ApoLp-III-DMPC complex was formed at an initial lipid to protein molar ratio of 67:1, with an apparent molecular mass of 642,000. Complexes cross-linked with dimethyl suberimidate indicate that there are a maximum of 6 apoLp-III molecules per disc. Circular dichroism experiments revealed that apoLp-III becomes essentially completely alpha-helical on formation of apoLp-III-DMPC complexes. Compared to apoLp-III in the lipid-free state, apoLp-III-DMPC complexes were relatively resistant to denaturation by guanidine HCl, displaying denaturation transitions with midpoints at 2.2 and 3.7 m guanidine HCl, respectively. The fluorescence excitation and emission spectra of ApoLp-III-DMPC complexes demonstrate a large enhancement of tyrosine fluorescence as compared to the lipid-free state, suggesting that a conformational change occurs when apoLp-III associates with a lipid surface. Denaturation of apoLp-III in the complex by guanidine HCl resulted in a tyrosine fluorescence level similar to that of lipid-free apoLp-III in the presence of guanidine HCl</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)41819-9</identifier><identifier>PMID: 8308032</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Apolipoproteins - chemistry ; Apolipoproteins - metabolism ; Biological and medical sciences ; Dimyristoylphosphatidylcholine - chemistry ; Dimyristoylphosphatidylcholine - metabolism ; Fundamental and applied biological sciences. Psychology ; HEMOLINFA ; HEMOLYMPHE ; In Vitro Techniques ; LECITHINE ; LECITINAS ; Lepidoptera ; Lipid Bilayers ; LIPOPROTEINAS ; LIPOPROTEINE ; Lipoproteins, myelin ; MANDUCA SEXTA ; Membrane Lipids - metabolism ; Microscopy, Electron ; Molecular Weight ; Moths ; Protein Binding ; Protein Conformation ; Protein Denaturation ; Protein Structure, Secondary ; PROTEINAS ; PROTEINE ; Proteins ; Spectrometry, Fluorescence ; Sphingidae</subject><ispartof>The Journal of biological chemistry, 1994-02, Vol.269 (6), p.4605-4612</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-b6d984db2750f4ee574ea46ef24f76d066d307db6d6ae1c1563a4b07049286e23</citedby><cites>FETCH-LOGICAL-c457t-b6d984db2750f4ee574ea46ef24f76d066d307db6d6ae1c1563a4b07049286e23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4045346$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8308032$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wientzek, M</creatorcontrib><creatorcontrib>Kay, C.M</creatorcontrib><creatorcontrib>Oikawa, K</creatorcontrib><creatorcontrib>Ryan, R.O</creatorcontrib><title>Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Apolipophorin-III (apoLp-III), a hemolymph protein of Manduca sexta, can reversibly associate with the surface of lipoprotein particles. In order to examine the lipid-associated form of apoLp-III, the present studies investigate the structure and properties of apoLp-III complexes with dimyristoylphosphatidylcholine (DMPC). Association of apoLp-III with DMPC vesicles results in the formation of uniform discs with an average diameter and width of 18.5 +/- 2.0 nm and 4.8 +/- 0.8 nm, respectively, as determined by electron microscopy. ApoLp-III-DMPC complexes analyzed by pore-limiting native gradient PAGE demonstrated that a single major species of complex was formed within a wide range of lipid to protein molar ratios (DMPC:apoLP-III; 13:1 to 360:1). Flotation equilibrium experiments, conducted in an analytical ultracentrifuge, confirmed that only one species of ApoLp-III-DMPC complex was formed at an initial lipid to protein molar ratio of 67:1, with an apparent molecular mass of 642,000. Complexes cross-linked with dimethyl suberimidate indicate that there are a maximum of 6 apoLp-III molecules per disc. Circular dichroism experiments revealed that apoLp-III becomes essentially completely alpha-helical on formation of apoLp-III-DMPC complexes. Compared to apoLp-III in the lipid-free state, apoLp-III-DMPC complexes were relatively resistant to denaturation by guanidine HCl, displaying denaturation transitions with midpoints at 2.2 and 3.7 m guanidine HCl, respectively. The fluorescence excitation and emission spectra of ApoLp-III-DMPC complexes demonstrate a large enhancement of tyrosine fluorescence as compared to the lipid-free state, suggesting that a conformational change occurs when apoLp-III associates with a lipid surface. Denaturation of apoLp-III in the complex by guanidine HCl resulted in a tyrosine fluorescence level similar to that of lipid-free apoLp-III in the presence of guanidine HCl</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Apolipoproteins - chemistry</subject><subject>Apolipoproteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Dimyristoylphosphatidylcholine - chemistry</subject><subject>Dimyristoylphosphatidylcholine - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HEMOLINFA</subject><subject>HEMOLYMPHE</subject><subject>In Vitro Techniques</subject><subject>LECITHINE</subject><subject>LECITINAS</subject><subject>Lepidoptera</subject><subject>Lipid Bilayers</subject><subject>LIPOPROTEINAS</subject><subject>LIPOPROTEINE</subject><subject>Lipoproteins, myelin</subject><subject>MANDUCA SEXTA</subject><subject>Membrane Lipids - metabolism</subject><subject>Microscopy, Electron</subject><subject>Molecular Weight</subject><subject>Moths</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Protein Structure, Secondary</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Proteins</subject><subject>Spectrometry, Fluorescence</subject><subject>Sphingidae</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9rFDEUB_AgSl2r_4BQCCKih6nJ5NfkWEvVhYKHWvAWssmbnchMMiazlf3vTbvLXs0lgfd5CXlfhC4ouaSEys93hLS00a3oPlL1idOO6kY_QytKOtYwQX89R6sTeYlelfKb1MU1PUNnHSMdYe0KLV9C9CFucepxiAXcgu2cxjCneUg5RLxer_GSsA_TPoeypP1YC2Ue7BL8fnRDtRHwA5TgRiiX-OYheIgOcJ8yttilWA9T1SnaEbvBxi28Ri96OxZ4c9zP0f3Xm5_X35vbH9_W11e3jeNCLc1Get1xv2mVID0HEIqD5RL6lvdKeiKlZ0T5yqQF6qiQzPINUfWPbSehZefow-HeOac_OyiLmUJxMI42QtoVo2SdUye7_0JajeKcVCgO0OVUSobezDlMNu8NJeYxFvMUi3mcuaHKPMVidO27OD6w20zgT13HHGr9_bFui7Njn210oZwYJ1wwLit7d2BD2A5_QwazCckNMJlWaiMNl0RU9PaAepuM3dbUzP2dFkRrytg_JpKqbw</recordid><startdate>19940211</startdate><enddate>19940211</enddate><creator>Wientzek, M</creator><creator>Kay, C.M</creator><creator>Oikawa, K</creator><creator>Ryan, R.O</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</scope><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>7SS</scope><scope>7X8</scope></search><sort><creationdate>19940211</creationdate><title>Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change</title><author>Wientzek, M ; Kay, C.M ; Oikawa, K ; Ryan, R.O</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-b6d984db2750f4ee574ea46ef24f76d066d307db6d6ae1c1563a4b07049286e23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Apolipoproteins - chemistry</topic><topic>Apolipoproteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>Dimyristoylphosphatidylcholine - chemistry</topic><topic>Dimyristoylphosphatidylcholine - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HEMOLINFA</topic><topic>HEMOLYMPHE</topic><topic>In Vitro Techniques</topic><topic>LECITHINE</topic><topic>LECITINAS</topic><topic>Lepidoptera</topic><topic>Lipid Bilayers</topic><topic>LIPOPROTEINAS</topic><topic>LIPOPROTEINE</topic><topic>Lipoproteins, myelin</topic><topic>MANDUCA SEXTA</topic><topic>Membrane Lipids - metabolism</topic><topic>Microscopy, Electron</topic><topic>Molecular Weight</topic><topic>Moths</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Protein Structure, Secondary</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>Proteins</topic><topic>Spectrometry, Fluorescence</topic><topic>Sphingidae</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wientzek, M</creatorcontrib><creatorcontrib>Kay, C.M</creatorcontrib><creatorcontrib>Oikawa, K</creatorcontrib><creatorcontrib>Ryan, R.O</creatorcontrib><collection>AGRIS</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>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wientzek, M</au><au>Kay, C.M</au><au>Oikawa, K</au><au>Ryan, R.O</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-02-11</date><risdate>1994</risdate><volume>269</volume><issue>6</issue><spage>4605</spage><epage>4612</epage><pages>4605-4612</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Apolipophorin-III (apoLp-III), a hemolymph protein of Manduca sexta, can reversibly associate with the surface of lipoprotein particles. In order to examine the lipid-associated form of apoLp-III, the present studies investigate the structure and properties of apoLp-III complexes with dimyristoylphosphatidylcholine (DMPC). Association of apoLp-III with DMPC vesicles results in the formation of uniform discs with an average diameter and width of 18.5 +/- 2.0 nm and 4.8 +/- 0.8 nm, respectively, as determined by electron microscopy. ApoLp-III-DMPC complexes analyzed by pore-limiting native gradient PAGE demonstrated that a single major species of complex was formed within a wide range of lipid to protein molar ratios (DMPC:apoLP-III; 13:1 to 360:1). Flotation equilibrium experiments, conducted in an analytical ultracentrifuge, confirmed that only one species of ApoLp-III-DMPC complex was formed at an initial lipid to protein molar ratio of 67:1, with an apparent molecular mass of 642,000. Complexes cross-linked with dimethyl suberimidate indicate that there are a maximum of 6 apoLp-III molecules per disc. Circular dichroism experiments revealed that apoLp-III becomes essentially completely alpha-helical on formation of apoLp-III-DMPC complexes. Compared to apoLp-III in the lipid-free state, apoLp-III-DMPC complexes were relatively resistant to denaturation by guanidine HCl, displaying denaturation transitions with midpoints at 2.2 and 3.7 m guanidine HCl, respectively. The fluorescence excitation and emission spectra of ApoLp-III-DMPC complexes demonstrate a large enhancement of tyrosine fluorescence as compared to the lipid-free state, suggesting that a conformational change occurs when apoLp-III associates with a lipid surface. Denaturation of apoLp-III in the complex by guanidine HCl resulted in a tyrosine fluorescence level similar to that of lipid-free apoLp-III in the presence of guanidine HCl</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8308032</pmid><doi>10.1016/S0021-9258(17)41819-9</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Animals Apolipoproteins - chemistry Apolipoproteins - metabolism Biological and medical sciences Dimyristoylphosphatidylcholine - chemistry Dimyristoylphosphatidylcholine - metabolism Fundamental and applied biological sciences. Psychology HEMOLINFA HEMOLYMPHE In Vitro Techniques LECITHINE LECITINAS Lepidoptera Lipid Bilayers LIPOPROTEINAS LIPOPROTEINE Lipoproteins, myelin MANDUCA SEXTA Membrane Lipids - metabolism Microscopy, Electron Molecular Weight Moths Protein Binding Protein Conformation Protein Denaturation Protein Structure, Secondary PROTEINAS PROTEINE Proteins Spectrometry, Fluorescence Sphingidae |
title | Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change |
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