Heat denaturation of pepsinogen in a water-ethanol mixture
The effect of ethanol and pH on thermodynamic parameters and cooperativity of pepsinogen heat denaturation was studied by scanning microcalorimetry. Addition of 20% ethanol decreases the protein denaturation temperature by 10.7°C at pH 6.4 and 15.8°C at pH 8.0. It also decreases the denaturation hea...
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| Veröffentlicht in: | FEBS letters 1995-01, Vol.357 (1), p.58-61 |
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| creator | Makarov, A.A. Protasevich, I.I. Bazhulina, N.P. Esipova, N.G. |
| description | The effect of ethanol and pH on thermodynamic parameters and cooperativity of pepsinogen heat denaturation was studied by scanning microcalorimetry. Addition of 20% ethanol decreases the protein denaturation temperature by 10.7°C at pH 6.4 and 15.8°C at pH 8.0. It also decreases the denaturation heat capacity increment from 5.8 to 4.2 kcal/K·mol. The dependences of calorimetric denaturation enthalpy on denaturation temperature both in water and 20% ethanol are linear and intersect at about 95°C. In 20% ethanol the pH shift from 5.9 to 8.0 results in a decreased number of cooperative domains in pepsinogen. This process causes no changes either in the secondary structure or in the local surroundings of aromatic amino acids. It is concluded that ethanol addition does not affect the cooperativity of pepsinogen denaturation substantially until the pH change provokes redistribution of charges in the protein molecule. |
| doi_str_mv | 10.1016/0014-5793(94)01308-N |
| format | Article |
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Addition of 20% ethanol decreases the protein denaturation temperature by 10.7°C at pH 6.4 and 15.8°C at pH 8.0. It also decreases the denaturation heat capacity increment from 5.8 to 4.2 kcal/K·mol. The dependences of calorimetric denaturation enthalpy on denaturation temperature both in water and 20% ethanol are linear and intersect at about 95°C. In 20% ethanol the pH shift from 5.9 to 8.0 results in a decreased number of cooperative domains in pepsinogen. This process causes no changes either in the secondary structure or in the local surroundings of aromatic amino acids. It is concluded that ethanol addition does not affect the cooperativity of pepsinogen denaturation substantially until the pH change provokes redistribution of charges in the protein molecule.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(94)01308-N</identifier><identifier>PMID: 8001679</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Calorimetry, Differential Scanning ; Ethanol ; Ethanol - pharmacology ; Heat denaturation ; Hot Temperature ; Hydrogen-Ion Concentration ; Pepsinogen ; Pepsinogens - chemistry ; Pepsinogens - drug effects ; Protein Denaturation ; Scanning microcalorimetry ; Water</subject><ispartof>FEBS letters, 1995-01, Vol.357 (1), p.58-61</ispartof><rights>1995</rights><rights>FEBS Letters 357 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466N-8fbd234dce614475113101907f58a71c16e8a191fc43b3f1be932e95e9082273</citedby><cites>FETCH-LOGICAL-c466N-8fbd234dce614475113101907f58a71c16e8a191fc43b3f1be932e95e9082273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(94)01308-N$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8001679$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Makarov, A.A.</creatorcontrib><creatorcontrib>Protasevich, I.I.</creatorcontrib><creatorcontrib>Bazhulina, N.P.</creatorcontrib><creatorcontrib>Esipova, N.G.</creatorcontrib><title>Heat denaturation of pepsinogen in a water-ethanol mixture</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The effect of ethanol and pH on thermodynamic parameters and cooperativity of pepsinogen heat denaturation was studied by scanning microcalorimetry. Addition of 20% ethanol decreases the protein denaturation temperature by 10.7°C at pH 6.4 and 15.8°C at pH 8.0. It also decreases the denaturation heat capacity increment from 5.8 to 4.2 kcal/K·mol. The dependences of calorimetric denaturation enthalpy on denaturation temperature both in water and 20% ethanol are linear and intersect at about 95°C. In 20% ethanol the pH shift from 5.9 to 8.0 results in a decreased number of cooperative domains in pepsinogen. This process causes no changes either in the secondary structure or in the local surroundings of aromatic amino acids. It is concluded that ethanol addition does not affect the cooperativity of pepsinogen denaturation substantially until the pH change provokes redistribution of charges in the protein molecule.</description><subject>Calorimetry, Differential Scanning</subject><subject>Ethanol</subject><subject>Ethanol - pharmacology</subject><subject>Heat denaturation</subject><subject>Hot Temperature</subject><subject>Hydrogen-Ion Concentration</subject><subject>Pepsinogen</subject><subject>Pepsinogens - chemistry</subject><subject>Pepsinogens - drug effects</subject><subject>Protein Denaturation</subject><subject>Scanning microcalorimetry</subject><subject>Water</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkDFPwzAQhS0EKqXwD0DKhGAI2LET2wxIULUUqSpLd8t1LmCUJsVOKf33OE3VETH5fO_du9OH0CXBdwST7B5jwuKUS3oj2S0mFIt4doT6RHAaU5aJY9Q_WE7RmfefOPwFkT3UE6HKuOyjhwnoJsqh0s3a6cbWVVQX0QpW3lb1O1SRrSIdbXQDLobmQ1d1GS3tTzDDOTopdOnhYv8O0Hw8mg8n8fTt5XX4NI0Ny7JZLIpFnlCWG8gIYzwlhIbzJeZFKjQnhmQgNJGkMIwuaEEWIGkCMgWJRZJwOkDXXezK1V9r8I1aWm-gLHUF9dorzrHgYVMwss5oXO29g0KtnF1qt1UEq5aYanGoFoeSTO2IqVkYu9rnrxdLyA9De0RBH3f6xpaw_VemGo-ek1Zo-5Ltuu2ixy4IAqxvC055Y6EykFsHplF5bf--9BcCwIxw</recordid><startdate>19950102</startdate><enddate>19950102</enddate><creator>Makarov, A.A.</creator><creator>Protasevich, I.I.</creator><creator>Bazhulina, N.P.</creator><creator>Esipova, N.G.</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>19950102</creationdate><title>Heat denaturation of pepsinogen in a water-ethanol mixture</title><author>Makarov, A.A. ; Protasevich, I.I. ; Bazhulina, N.P. ; Esipova, N.G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466N-8fbd234dce614475113101907f58a71c16e8a191fc43b3f1be932e95e9082273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Calorimetry, Differential Scanning</topic><topic>Ethanol</topic><topic>Ethanol - pharmacology</topic><topic>Heat denaturation</topic><topic>Hot Temperature</topic><topic>Hydrogen-Ion Concentration</topic><topic>Pepsinogen</topic><topic>Pepsinogens - chemistry</topic><topic>Pepsinogens - drug effects</topic><topic>Protein Denaturation</topic><topic>Scanning microcalorimetry</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Makarov, A.A.</creatorcontrib><creatorcontrib>Protasevich, I.I.</creatorcontrib><creatorcontrib>Bazhulina, N.P.</creatorcontrib><creatorcontrib>Esipova, N.G.</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>Makarov, A.A.</au><au>Protasevich, I.I.</au><au>Bazhulina, N.P.</au><au>Esipova, N.G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heat denaturation of pepsinogen in a water-ethanol mixture</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-01-02</date><risdate>1995</risdate><volume>357</volume><issue>1</issue><spage>58</spage><epage>61</epage><pages>58-61</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The effect of ethanol and pH on thermodynamic parameters and cooperativity of pepsinogen heat denaturation was studied by scanning microcalorimetry. Addition of 20% ethanol decreases the protein denaturation temperature by 10.7°C at pH 6.4 and 15.8°C at pH 8.0. It also decreases the denaturation heat capacity increment from 5.8 to 4.2 kcal/K·mol. The dependences of calorimetric denaturation enthalpy on denaturation temperature both in water and 20% ethanol are linear and intersect at about 95°C. In 20% ethanol the pH shift from 5.9 to 8.0 results in a decreased number of cooperative domains in pepsinogen. This process causes no changes either in the secondary structure or in the local surroundings of aromatic amino acids. It is concluded that ethanol addition does not affect the cooperativity of pepsinogen denaturation substantially until the pH change provokes redistribution of charges in the protein molecule.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8001679</pmid><doi>10.1016/0014-5793(94)01308-N</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Calorimetry, Differential Scanning Ethanol Ethanol - pharmacology Heat denaturation Hot Temperature Hydrogen-Ion Concentration Pepsinogen Pepsinogens - chemistry Pepsinogens - drug effects Protein Denaturation Scanning microcalorimetry Water |
| title | Heat denaturation of pepsinogen in a water-ethanol mixture |
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