Further studies on the temperature dependence of the binding of testosterone to human pregnancy plasma proteins
The binding of testosterone by pregnancy plasma proteins has been studied by a new equilibrium dialysis system. The temperature dependence on the association constant has been investigated and the enthalpy change ΔH and entropy change ΔS have been calculated. By a computer optimization program, the...
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| Veröffentlicht in: | Steroids 1973-03, Vol.21 (3), p.423-431 |
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| creator | Lutz, R.A. Lutz-Ewan, L. Weder, H.G. |
| description | The binding of testosterone by pregnancy plasma proteins has been studied by a new equilibrium dialysis system. The temperature dependence on the association constant has been investigated and the enthalpy change ΔH and entropy change ΔS have been calculated.
By a computer optimization program, the binding constant of the high affinity testosterone binding protein has been estimated from Scatchard plots. The binding reactions were carried out at 5°, 25° and 37° C. The corresponding values were 3.1.10 1.2.10
9 and 7.2.10
8 liter/mole. The resulting enthalpy and entropy changes were −2.0 kcal/mole and 35.0 cal/(mole.degree) respectively.
It can be concluded that the binding of testosterone to the specific binding protein is an exothermic reaction and is stabilized by hydrophobic binding forces. |
| doi_str_mv | 10.1016/0039-128X(73)90034-2 |
| format | Article |
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By a computer optimization program, the binding constant of the high affinity testosterone binding protein has been estimated from Scatchard plots. The binding reactions were carried out at 5°, 25° and 37° C. The corresponding values were 3.1.10 1.2.10
9 and 7.2.10
8 liter/mole. The resulting enthalpy and entropy changes were −2.0 kcal/mole and 35.0 cal/(mole.degree) respectively.
It can be concluded that the binding of testosterone to the specific binding protein is an exothermic reaction and is stabilized by hydrophobic binding forces.</description><identifier>ISSN: 0039-128X</identifier><identifier>EISSN: 1878-5867</identifier><identifier>DOI: 10.1016/0039-128X(73)90034-2</identifier><identifier>PMID: 4693735</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>1, 3, 5-Estratriene-3, 17β-diol ; 17β-Hydroxy-4-androstene-3-one ; 17β-Hydroxy-5α-androstan-3-one ; Blood Proteins ; Dialysis ; dihydrotestosterone ; estradiol ; Female ; Humans ; Mathematics ; Pregnancy ; Protein Binding ; Temperature ; testosterone ; Testosterone - blood ; Tritium</subject><ispartof>Steroids, 1973-03, Vol.21 (3), p.423-431</ispartof><rights>1973</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-856ce88389e2fc7b0d99278f5616c2d8055f3d4a2ddcbdfd3982c31b0cc3c0af3</citedby><cites>FETCH-LOGICAL-c357t-856ce88389e2fc7b0d99278f5616c2d8055f3d4a2ddcbdfd3982c31b0cc3c0af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0039-128X(73)90034-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4693735$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lutz, R.A.</creatorcontrib><creatorcontrib>Lutz-Ewan, L.</creatorcontrib><creatorcontrib>Weder, H.G.</creatorcontrib><title>Further studies on the temperature dependence of the binding of testosterone to human pregnancy plasma proteins</title><title>Steroids</title><addtitle>Steroids</addtitle><description>The binding of testosterone by pregnancy plasma proteins has been studied by a new equilibrium dialysis system. The temperature dependence on the association constant has been investigated and the enthalpy change ΔH and entropy change ΔS have been calculated.
By a computer optimization program, the binding constant of the high affinity testosterone binding protein has been estimated from Scatchard plots. The binding reactions were carried out at 5°, 25° and 37° C. The corresponding values were 3.1.10 1.2.10
9 and 7.2.10
8 liter/mole. The resulting enthalpy and entropy changes were −2.0 kcal/mole and 35.0 cal/(mole.degree) respectively.
It can be concluded that the binding of testosterone to the specific binding protein is an exothermic reaction and is stabilized by hydrophobic binding forces.</description><subject>1, 3, 5-Estratriene-3, 17β-diol</subject><subject>17β-Hydroxy-4-androstene-3-one</subject><subject>17β-Hydroxy-5α-androstan-3-one</subject><subject>Blood Proteins</subject><subject>Dialysis</subject><subject>dihydrotestosterone</subject><subject>estradiol</subject><subject>Female</subject><subject>Humans</subject><subject>Mathematics</subject><subject>Pregnancy</subject><subject>Protein Binding</subject><subject>Temperature</subject><subject>testosterone</subject><subject>Testosterone - blood</subject><subject>Tritium</subject><issn>0039-128X</issn><issn>1878-5867</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAUhYMoOo7-A4WsRBfVPKZtuhFEfMGAGwV3IU1uNTJNapIK_nvTmcGlq3Byzrk3-RA6oeSSElpdEcKbgjLxdl7ziyarRcF20IyKWhSlqOpdNPuLHKDDGD8JIRVv2D7aX1QNr3k5Q_5-DOkDAo5pNBYi9g5njRP0AwSVxgDYwADOgNOAfbd2W-uMde9rCTH5mCB4l1sef4y9cngI8O6U0z94WKnYq3zhE1gXj9Bep1YRjrfnHL3e373cPhbL54en25tloXlZp0KUlQYhuGiAdbpuiWkaVouurGilmRGkLDtuFooZo1vTGd4IpjltidZcE9XxOTrbzM2Lv8b8RtnbqGG1Ug78GKWgohSUsxxcbII6-BgDdHIItlfhR1IiJ85ygigniLLmcs1ZTrXT7fyx7cH8lbZgs3-98SF_8ttCkFHbCaGxAXSSxtv_F_wC1zCPqA</recordid><startdate>197303</startdate><enddate>197303</enddate><creator>Lutz, R.A.</creator><creator>Lutz-Ewan, L.</creator><creator>Weder, H.G.</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>197303</creationdate><title>Further studies on the temperature dependence of the binding of testosterone to human pregnancy plasma proteins</title><author>Lutz, R.A. ; Lutz-Ewan, L. ; Weder, H.G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-856ce88389e2fc7b0d99278f5616c2d8055f3d4a2ddcbdfd3982c31b0cc3c0af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>1, 3, 5-Estratriene-3, 17β-diol</topic><topic>17β-Hydroxy-4-androstene-3-one</topic><topic>17β-Hydroxy-5α-androstan-3-one</topic><topic>Blood Proteins</topic><topic>Dialysis</topic><topic>dihydrotestosterone</topic><topic>estradiol</topic><topic>Female</topic><topic>Humans</topic><topic>Mathematics</topic><topic>Pregnancy</topic><topic>Protein Binding</topic><topic>Temperature</topic><topic>testosterone</topic><topic>Testosterone - blood</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lutz, R.A.</creatorcontrib><creatorcontrib>Lutz-Ewan, L.</creatorcontrib><creatorcontrib>Weder, H.G.</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>Steroids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lutz, R.A.</au><au>Lutz-Ewan, L.</au><au>Weder, H.G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Further studies on the temperature dependence of the binding of testosterone to human pregnancy plasma proteins</atitle><jtitle>Steroids</jtitle><addtitle>Steroids</addtitle><date>1973-03</date><risdate>1973</risdate><volume>21</volume><issue>3</issue><spage>423</spage><epage>431</epage><pages>423-431</pages><issn>0039-128X</issn><eissn>1878-5867</eissn><abstract>The binding of testosterone by pregnancy plasma proteins has been studied by a new equilibrium dialysis system. The temperature dependence on the association constant has been investigated and the enthalpy change ΔH and entropy change ΔS have been calculated.
By a computer optimization program, the binding constant of the high affinity testosterone binding protein has been estimated from Scatchard plots. The binding reactions were carried out at 5°, 25° and 37° C. The corresponding values were 3.1.10 1.2.10
9 and 7.2.10
8 liter/mole. The resulting enthalpy and entropy changes were −2.0 kcal/mole and 35.0 cal/(mole.degree) respectively.
It can be concluded that the binding of testosterone to the specific binding protein is an exothermic reaction and is stabilized by hydrophobic binding forces.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4693735</pmid><doi>10.1016/0039-128X(73)90034-2</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0039-128X |
| ispartof | Steroids, 1973-03, Vol.21 (3), p.423-431 |
| issn | 0039-128X 1878-5867 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | 1, 3, 5-Estratriene-3, 17β-diol 17β-Hydroxy-4-androstene-3-one 17β-Hydroxy-5α-androstan-3-one Blood Proteins Dialysis dihydrotestosterone estradiol Female Humans Mathematics Pregnancy Protein Binding Temperature testosterone Testosterone - blood Tritium |
| title | Further studies on the temperature dependence of the binding of testosterone to human pregnancy plasma proteins |
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