Cycloamylose as an efficient artificial chaperone for protein refolding
High molecular weight cyclic α-1,4-glucan (referred to as cycloamylose) exhibited an artificial chaperone property toward three enzymes in different categories. The inclusion properties of cycloamylose effectively accommodated detergents, which keep the chemically denatured enzymes from aggregation,...
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| Veröffentlicht in: | FEBS letters 2000-12, Vol.486 (2), p.131-135 |
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| creator | Machida, Sachiko Ogawa, Setsuko Xiaohua, Shi Takaha, Takeshi Fujii, Kazutoshi Hayashi, Kiyoshi |
| description | High molecular weight cyclic α-1,4-glucan (referred to as cycloamylose) exhibited an artificial chaperone property toward three enzymes in different categories. The inclusion properties of cycloamylose effectively accommodated detergents, which keep the chemically denatured enzymes from aggregation, and promoted proper protein folding. Chemically denatured citrate synthase was refolded and completely recovered it’s enzymatic activity after dilution with polyoxyethylenesorbitan buffer followed by cycloamylose treatment. The refolding was completed within 2 h, and the activity of the refolded citrate synthase was quite stable. Cycloamylose also promoted the refolding of denatured carbonic anhydrase B and denatured lysozyme of a reduced form. |
| doi_str_mv | 10.1016/S0014-5793(00)02258-4 |
| format | Article |
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The inclusion properties of cycloamylose effectively accommodated detergents, which keep the chemically denatured enzymes from aggregation, and promoted proper protein folding. Chemically denatured citrate synthase was refolded and completely recovered it’s enzymatic activity after dilution with polyoxyethylenesorbitan buffer followed by cycloamylose treatment. The refolding was completed within 2 h, and the activity of the refolded citrate synthase was quite stable. Cycloamylose also promoted the refolding of denatured carbonic anhydrase B and denatured lysozyme of a reduced form.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(00)02258-4</identifier><identifier>PMID: 11113453</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Artificial chaperone ; Carbonic anhydrase B ; Carbonic Anhydrases - chemistry ; Carbonic Anhydrases - metabolism ; Citrate (si)-Synthase - chemistry ; Citrate (si)-Synthase - metabolism ; Citrate synthase ; Cycloamylose ; Cyclodextrins - chemistry ; Detergents - chemistry ; Glucans - chemistry ; Lysozyme ; Molecular Chaperones - chemistry ; Muramidase - chemistry ; Muramidase - metabolism ; Protein Denaturation ; Protein Folding ; Refolding ; Swine</subject><ispartof>FEBS letters, 2000-12, Vol.486 (2), p.131-135</ispartof><rights>2000 Federation of European Biochemical Societies</rights><rights>FEBS Letters 486 (2000) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5394-31bc1ecdfa1f8a1248e184164d318da809a93036fdc8e553f061ce91882bd08a3</citedby><cites>FETCH-LOGICAL-c5394-31bc1ecdfa1f8a1248e184164d318da809a93036fdc8e553f061ce91882bd08a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2800%2902258-4$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(00)02258-4$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3536,27903,27904,45553,45554,45974,46388,46812</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11113453$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Machida, Sachiko</creatorcontrib><creatorcontrib>Ogawa, Setsuko</creatorcontrib><creatorcontrib>Xiaohua, Shi</creatorcontrib><creatorcontrib>Takaha, Takeshi</creatorcontrib><creatorcontrib>Fujii, Kazutoshi</creatorcontrib><creatorcontrib>Hayashi, Kiyoshi</creatorcontrib><title>Cycloamylose as an efficient artificial chaperone for protein refolding</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>High molecular weight cyclic α-1,4-glucan (referred to as cycloamylose) exhibited an artificial chaperone property toward three enzymes in different categories. The inclusion properties of cycloamylose effectively accommodated detergents, which keep the chemically denatured enzymes from aggregation, and promoted proper protein folding. Chemically denatured citrate synthase was refolded and completely recovered it’s enzymatic activity after dilution with polyoxyethylenesorbitan buffer followed by cycloamylose treatment. The refolding was completed within 2 h, and the activity of the refolded citrate synthase was quite stable. Cycloamylose also promoted the refolding of denatured carbonic anhydrase B and denatured lysozyme of a reduced form.</description><subject>Animals</subject><subject>Artificial chaperone</subject><subject>Carbonic anhydrase B</subject><subject>Carbonic Anhydrases - chemistry</subject><subject>Carbonic Anhydrases - metabolism</subject><subject>Citrate (si)-Synthase - chemistry</subject><subject>Citrate (si)-Synthase - metabolism</subject><subject>Citrate synthase</subject><subject>Cycloamylose</subject><subject>Cyclodextrins - chemistry</subject><subject>Detergents - chemistry</subject><subject>Glucans - chemistry</subject><subject>Lysozyme</subject><subject>Molecular Chaperones - chemistry</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - metabolism</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Refolding</subject><subject>Swine</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkctOwzAQRS0EgvL4BFBWCBYBT-ykzgpBBQWpEgtgbbn2GIzSuNgpqH-P01awBG_8mDt3ro4JOQZ6ARSqyydKgeflsGZnlJ7ToihFzrfIAMSQ5YxXYpsMfiR7ZD_Gd5ruAupdsgdpMV6yARmPlrrxarZsfMRMxUy1GVrrtMO2y1ToXH9WTabf1ByDbzGzPmTz4Dt0bRbQ-sa49vWQ7FjVRDza7Afk5e72eXSfTx7HD6PrSa5LVvOcwVQDamMVWKGg4AJBcKi4YSCMErRWNaOsskYLLEtmaQUaaxCimBoqFDsgp2vflOBjgbGTMxc1No1q0S-iHBa8GvJCJGG5FurgY0w55Ty4mQpLCVT2BOWKoOzxSErliqDkqe9kM2AxnaH57dogS4L7teDLNbj8n6u8u70pVpW-kP6hf-5nXa2tMBH7dBhk7LlrNC6g7qTx7o-03zvOk9Y</recordid><startdate>20001208</startdate><enddate>20001208</enddate><creator>Machida, Sachiko</creator><creator>Ogawa, Setsuko</creator><creator>Xiaohua, Shi</creator><creator>Takaha, Takeshi</creator><creator>Fujii, Kazutoshi</creator><creator>Hayashi, Kiyoshi</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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></search><sort><creationdate>20001208</creationdate><title>Cycloamylose as an efficient artificial chaperone for protein refolding</title><author>Machida, Sachiko ; Ogawa, Setsuko ; Xiaohua, Shi ; Takaha, Takeshi ; Fujii, Kazutoshi ; Hayashi, Kiyoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5394-31bc1ecdfa1f8a1248e184164d318da809a93036fdc8e553f061ce91882bd08a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Artificial chaperone</topic><topic>Carbonic anhydrase B</topic><topic>Carbonic Anhydrases - chemistry</topic><topic>Carbonic Anhydrases - metabolism</topic><topic>Citrate (si)-Synthase - chemistry</topic><topic>Citrate (si)-Synthase - metabolism</topic><topic>Citrate synthase</topic><topic>Cycloamylose</topic><topic>Cyclodextrins - chemistry</topic><topic>Detergents - chemistry</topic><topic>Glucans - chemistry</topic><topic>Lysozyme</topic><topic>Molecular Chaperones - chemistry</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - metabolism</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Refolding</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Machida, Sachiko</creatorcontrib><creatorcontrib>Ogawa, Setsuko</creatorcontrib><creatorcontrib>Xiaohua, Shi</creatorcontrib><creatorcontrib>Takaha, Takeshi</creatorcontrib><creatorcontrib>Fujii, Kazutoshi</creatorcontrib><creatorcontrib>Hayashi, Kiyoshi</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Machida, Sachiko</au><au>Ogawa, Setsuko</au><au>Xiaohua, Shi</au><au>Takaha, Takeshi</au><au>Fujii, Kazutoshi</au><au>Hayashi, Kiyoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cycloamylose as an efficient artificial chaperone for protein refolding</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2000-12-08</date><risdate>2000</risdate><volume>486</volume><issue>2</issue><spage>131</spage><epage>135</epage><pages>131-135</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>High molecular weight cyclic α-1,4-glucan (referred to as cycloamylose) exhibited an artificial chaperone property toward three enzymes in different categories. 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| ispartof | FEBS letters, 2000-12, Vol.486 (2), p.131-135 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Artificial chaperone Carbonic anhydrase B Carbonic Anhydrases - chemistry Carbonic Anhydrases - metabolism Citrate (si)-Synthase - chemistry Citrate (si)-Synthase - metabolism Citrate synthase Cycloamylose Cyclodextrins - chemistry Detergents - chemistry Glucans - chemistry Lysozyme Molecular Chaperones - chemistry Muramidase - chemistry Muramidase - metabolism Protein Denaturation Protein Folding Refolding Swine |
| title | Cycloamylose as an efficient artificial chaperone for protein refolding |
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