Measurement of protein denaturation in human synovial fluid and its analogs using differential scanning calorimetry
Differential scanning calorimetry (DSC) was used to evaluate the thermal transitions associated with protein constituents of synovial fluid samples from three individuals with osteoarthritis. Analysis of the multi-component DSC curves revealed that major endothermic transitions of synovial fluid occ...
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description | Differential scanning calorimetry (DSC) was used to evaluate the thermal transitions associated with protein constituents of synovial fluid samples from three individuals with osteoarthritis. Analysis of the multi-component DSC curves revealed that major endothermic transitions of synovial fluid occur between 60 and 80 °C and can be resolved into three peaks, likely due to the unfolding of human serum albumin and immunoglobulins, and that the enthalpies of these transitions can be quantified in terms of their relative contribution to the total system enthalpy. DSC was also used to analyze a solution of bovine calf serum, a lubricant used in simulator wear testing of joint replacement implants, and the resulting endothermic transitions occurred in a temperature range relevant to that produced by frictional heat during such wear simulator testing. Results of this study indicate a new application for DSC as a direct method for studying thermal stabilities of both bovine calf serum and synovial fluid. The use of DSC is proposed as a diagnostic tool to detect altered thermal properties or protein concentrations indicative of a diseased or injured state, and as a development tool to test the efficacy of additives in controlling protein denaturation associated with increased wear in joint replacement implants. |
doi_str_mv | 10.1007/s10973-010-0794-9 |
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Analysis of the multi-component DSC curves revealed that major endothermic transitions of synovial fluid occur between 60 and 80 °C and can be resolved into three peaks, likely due to the unfolding of human serum albumin and immunoglobulins, and that the enthalpies of these transitions can be quantified in terms of their relative contribution to the total system enthalpy. DSC was also used to analyze a solution of bovine calf serum, a lubricant used in simulator wear testing of joint replacement implants, and the resulting endothermic transitions occurred in a temperature range relevant to that produced by frictional heat during such wear simulator testing. Results of this study indicate a new application for DSC as a direct method for studying thermal stabilities of both bovine calf serum and synovial fluid. The use of DSC is proposed as a diagnostic tool to detect altered thermal properties or protein concentrations indicative of a diseased or injured state, and as a development tool to test the efficacy of additives in controlling protein denaturation associated with increased wear in joint replacement implants.</description><identifier>ISSN: 1388-6150</identifier><identifier>EISSN: 1588-2926</identifier><identifier>EISSN: 1572-8943</identifier><identifier>DOI: 10.1007/s10973-010-0794-9</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Analysis ; Analytical Chemistry ; Biological and medical sciences ; Calorimetry ; Cattle ; Chemistry ; Chemistry and Materials Science ; Denaturation ; Diseases of the osteoarticular system ; Inorganic Chemistry ; Joint replacement ; Lubrication and lubricants ; Measurement ; Measurement Science and Instrumentation ; Medical sciences ; Osteoarthritis ; Physical Chemistry ; Polymer Sciences ; Proteins ; Thermal properties</subject><ispartof>Journal of thermal analysis and calorimetry, 2010-10, Vol.102 (1), p.99-106</ispartof><rights>Akadémiai Kiadó, Budapest, Hungary 2010</rights><rights>2015 INIST-CNRS</rights><rights>COPYRIGHT 2010 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-227c5788f69c2e894112fae821818f2b21b590a302e2d449b89e2ef81da1e8603</citedby><cites>FETCH-LOGICAL-c419t-227c5788f69c2e894112fae821818f2b21b590a302e2d449b89e2ef81da1e8603</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10973-010-0794-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10973-010-0794-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23228036$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Briere, Lee-Ann K.</creatorcontrib><creatorcontrib>Brandt, Jan-M.</creatorcontrib><creatorcontrib>Medley, John B.</creatorcontrib><title>Measurement of protein denaturation in human synovial fluid and its analogs using differential scanning calorimetry</title><title>Journal of thermal analysis and calorimetry</title><addtitle>J Therm Anal Calorim</addtitle><description>Differential scanning calorimetry (DSC) was used to evaluate the thermal transitions associated with protein constituents of synovial fluid samples from three individuals with osteoarthritis. Analysis of the multi-component DSC curves revealed that major endothermic transitions of synovial fluid occur between 60 and 80 °C and can be resolved into three peaks, likely due to the unfolding of human serum albumin and immunoglobulins, and that the enthalpies of these transitions can be quantified in terms of their relative contribution to the total system enthalpy. DSC was also used to analyze a solution of bovine calf serum, a lubricant used in simulator wear testing of joint replacement implants, and the resulting endothermic transitions occurred in a temperature range relevant to that produced by frictional heat during such wear simulator testing. Results of this study indicate a new application for DSC as a direct method for studying thermal stabilities of both bovine calf serum and synovial fluid. The use of DSC is proposed as a diagnostic tool to detect altered thermal properties or protein concentrations indicative of a diseased or injured state, and as a development tool to test the efficacy of additives in controlling protein denaturation associated with increased wear in joint replacement implants.</description><subject>Analysis</subject><subject>Analytical Chemistry</subject><subject>Biological and medical sciences</subject><subject>Calorimetry</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Denaturation</subject><subject>Diseases of the osteoarticular system</subject><subject>Inorganic Chemistry</subject><subject>Joint replacement</subject><subject>Lubrication and lubricants</subject><subject>Measurement</subject><subject>Measurement Science and Instrumentation</subject><subject>Medical sciences</subject><subject>Osteoarthritis</subject><subject>Physical Chemistry</subject><subject>Polymer Sciences</subject><subject>Proteins</subject><subject>Thermal properties</subject><issn>1388-6150</issn><issn>1588-2926</issn><issn>1572-8943</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNp9kU1rFTEUhgexYGn7A7oLiAsXU5PMV7IsRWuhRbB2Hc7NnIyRmeSSkxHvvzeXEeGCSBbnI8_7Ls5bVdeC3wjOhw8kuB6amgte80G3tX5VnYtOqVpq2b8ufVP6XnT8TXVF5HdcCt7rTunzip4QaE24YMgsOrZPMaMPbMQAeU2QfQyszN_XBQKjQ4g_PczMzasfGYSR-UylwhwnYiv5MLHRO4ep-B1BshDCcWsLkvyCOR0uqzMHM-HVn3pRvXz6-O3uc_345f7h7vaxtq3QuZZysN2glOu1lah0K4R0gEoKJZSTOyl2nebQcIlybFu9UxolOiVGEKh63lxUbzffCWY0PriYE9jFkzW3TadlVxzbQt38gypvxMXbGND5sj8RvD8RFCbjrzzBSmQenr-esmJjbYpECZ3ZlyNAOhjBzTE7s2VnSnbmmJ3RRfNu0-yhXG92CYL19FcoGykVb_rCyY2j8hUmTOZHXFOJgv5j_hs6mqi6</recordid><startdate>20101001</startdate><enddate>20101001</enddate><creator>Briere, Lee-Ann K.</creator><creator>Brandt, Jan-M.</creator><creator>Medley, John B.</creator><general>Springer Netherlands</general><general>Springer</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope></search><sort><creationdate>20101001</creationdate><title>Measurement of protein denaturation in human synovial fluid and its analogs using differential scanning calorimetry</title><author>Briere, Lee-Ann K. ; Brandt, Jan-M. ; Medley, John B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-227c5788f69c2e894112fae821818f2b21b590a302e2d449b89e2ef81da1e8603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Analysis</topic><topic>Analytical Chemistry</topic><topic>Biological and medical sciences</topic><topic>Calorimetry</topic><topic>Cattle</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Denaturation</topic><topic>Diseases of the osteoarticular system</topic><topic>Inorganic Chemistry</topic><topic>Joint replacement</topic><topic>Lubrication and lubricants</topic><topic>Measurement</topic><topic>Measurement Science and Instrumentation</topic><topic>Medical sciences</topic><topic>Osteoarthritis</topic><topic>Physical Chemistry</topic><topic>Polymer Sciences</topic><topic>Proteins</topic><topic>Thermal properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Briere, Lee-Ann K.</creatorcontrib><creatorcontrib>Brandt, Jan-M.</creatorcontrib><creatorcontrib>Medley, John B.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><jtitle>Journal of thermal analysis and calorimetry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Briere, Lee-Ann K.</au><au>Brandt, Jan-M.</au><au>Medley, John B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Measurement of protein denaturation in human synovial fluid and its analogs using differential scanning calorimetry</atitle><jtitle>Journal of thermal analysis and calorimetry</jtitle><stitle>J Therm Anal Calorim</stitle><date>2010-10-01</date><risdate>2010</risdate><volume>102</volume><issue>1</issue><spage>99</spage><epage>106</epage><pages>99-106</pages><issn>1388-6150</issn><eissn>1588-2926</eissn><eissn>1572-8943</eissn><abstract>Differential scanning calorimetry (DSC) was used to evaluate the thermal transitions associated with protein constituents of synovial fluid samples from three individuals with osteoarthritis. Analysis of the multi-component DSC curves revealed that major endothermic transitions of synovial fluid occur between 60 and 80 °C and can be resolved into three peaks, likely due to the unfolding of human serum albumin and immunoglobulins, and that the enthalpies of these transitions can be quantified in terms of their relative contribution to the total system enthalpy. DSC was also used to analyze a solution of bovine calf serum, a lubricant used in simulator wear testing of joint replacement implants, and the resulting endothermic transitions occurred in a temperature range relevant to that produced by frictional heat during such wear simulator testing. Results of this study indicate a new application for DSC as a direct method for studying thermal stabilities of both bovine calf serum and synovial fluid. The use of DSC is proposed as a diagnostic tool to detect altered thermal properties or protein concentrations indicative of a diseased or injured state, and as a development tool to test the efficacy of additives in controlling protein denaturation associated with increased wear in joint replacement implants.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><doi>10.1007/s10973-010-0794-9</doi><tpages>8</tpages></addata></record> |
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subjects | Analysis Analytical Chemistry Biological and medical sciences Calorimetry Cattle Chemistry Chemistry and Materials Science Denaturation Diseases of the osteoarticular system Inorganic Chemistry Joint replacement Lubrication and lubricants Measurement Measurement Science and Instrumentation Medical sciences Osteoarthritis Physical Chemistry Polymer Sciences Proteins Thermal properties |
title | Measurement of protein denaturation in human synovial fluid and its analogs using differential scanning calorimetry |
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