RETRACTED ARTICLE: Thermodynamic study on the interaction of cyanide ion and jack bean urease at different temperatures
Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JB...
Ausführliche Beschreibung
Autor*in: |
Rezaei Behbehani, G. [verfasserIn] |
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Format: |
Artikel |
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Sprache: |
Englisch |
Erschienen: |
2009 |
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Schlagwörter: |
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Anmerkung: |
© Akadémiai Kiadó, Budapest, Hungary 2009 |
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Übergeordnetes Werk: |
Enthalten in: Journal of thermal analysis and calorimetry - Springer Netherlands, 1998, 100(2009), 3 vom: 28. Aug., Seite 1079-1083 |
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Übergeordnetes Werk: |
volume:100 ; year:2009 ; number:3 ; day:28 ; month:08 ; pages:1079-1083 |
Links: |
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DOI / URN: |
10.1007/s10973-009-0384-x |
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OLC2049799713 |
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10.1007/s10973-009-0384-x doi (DE-627)OLC2049799713 (DE-He213)s10973-009-0384-x-p DE-627 ger DE-627 rakwb eng 660 VZ Rezaei Behbehani, G. verfasserin aut RETRACTED ARTICLE: Thermodynamic study on the interaction of cyanide ion and jack bean urease at different temperatures 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2009 Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JBU complexation have been calculated. It was found that in the low and high concentrations of the cyanide ions, the JBU structure was destabilized, resulting in a decrease in its biological activity. Jack bean urease Cyanide ion Isothermal titration calorimetry Binding parameters Solvation model Saboury, A. A. aut Mohebbian, M. aut Abedini, J. aut Tahmasebi Sarvestani, S. aut Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 100(2009), 3 vom: 28. Aug., Seite 1079-1083 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:100 year:2009 number:3 day:28 month:08 pages:1079-1083 https://doi.org/10.1007/s10973-009-0384-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 100 2009 3 28 08 1079-1083 |
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10.1007/s10973-009-0384-x doi (DE-627)OLC2049799713 (DE-He213)s10973-009-0384-x-p DE-627 ger DE-627 rakwb eng 660 VZ Rezaei Behbehani, G. verfasserin aut RETRACTED ARTICLE: Thermodynamic study on the interaction of cyanide ion and jack bean urease at different temperatures 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2009 Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JBU complexation have been calculated. It was found that in the low and high concentrations of the cyanide ions, the JBU structure was destabilized, resulting in a decrease in its biological activity. Jack bean urease Cyanide ion Isothermal titration calorimetry Binding parameters Solvation model Saboury, A. A. aut Mohebbian, M. aut Abedini, J. aut Tahmasebi Sarvestani, S. aut Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 100(2009), 3 vom: 28. Aug., Seite 1079-1083 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:100 year:2009 number:3 day:28 month:08 pages:1079-1083 https://doi.org/10.1007/s10973-009-0384-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 100 2009 3 28 08 1079-1083 |
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10.1007/s10973-009-0384-x doi (DE-627)OLC2049799713 (DE-He213)s10973-009-0384-x-p DE-627 ger DE-627 rakwb eng 660 VZ Rezaei Behbehani, G. verfasserin aut RETRACTED ARTICLE: Thermodynamic study on the interaction of cyanide ion and jack bean urease at different temperatures 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2009 Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JBU complexation have been calculated. It was found that in the low and high concentrations of the cyanide ions, the JBU structure was destabilized, resulting in a decrease in its biological activity. Jack bean urease Cyanide ion Isothermal titration calorimetry Binding parameters Solvation model Saboury, A. A. aut Mohebbian, M. aut Abedini, J. aut Tahmasebi Sarvestani, S. aut Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 100(2009), 3 vom: 28. Aug., Seite 1079-1083 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:100 year:2009 number:3 day:28 month:08 pages:1079-1083 https://doi.org/10.1007/s10973-009-0384-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 100 2009 3 28 08 1079-1083 |
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10.1007/s10973-009-0384-x doi (DE-627)OLC2049799713 (DE-He213)s10973-009-0384-x-p DE-627 ger DE-627 rakwb eng 660 VZ Rezaei Behbehani, G. verfasserin aut RETRACTED ARTICLE: Thermodynamic study on the interaction of cyanide ion and jack bean urease at different temperatures 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2009 Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JBU complexation have been calculated. It was found that in the low and high concentrations of the cyanide ions, the JBU structure was destabilized, resulting in a decrease in its biological activity. Jack bean urease Cyanide ion Isothermal titration calorimetry Binding parameters Solvation model Saboury, A. A. aut Mohebbian, M. aut Abedini, J. aut Tahmasebi Sarvestani, S. aut Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 100(2009), 3 vom: 28. Aug., Seite 1079-1083 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:100 year:2009 number:3 day:28 month:08 pages:1079-1083 https://doi.org/10.1007/s10973-009-0384-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 100 2009 3 28 08 1079-1083 |
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Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JBU complexation have been calculated. It was found that in the low and high concentrations of the cyanide ions, the JBU structure was destabilized, resulting in a decrease in its biological activity. © Akadémiai Kiadó, Budapest, Hungary 2009 |
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Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JBU complexation have been calculated. It was found that in the low and high concentrations of the cyanide ions, the JBU structure was destabilized, resulting in a decrease in its biological activity. © Akadémiai Kiadó, Budapest, Hungary 2009 |
abstract_unstemmed |
Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JBU complexation have been calculated. It was found that in the low and high concentrations of the cyanide ions, the JBU structure was destabilized, resulting in a decrease in its biological activity. © Akadémiai Kiadó, Budapest, Hungary 2009 |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">OLC2049799713</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230503165723.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">200820s2009 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s10973-009-0384-x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC2049799713</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-He213)s10973-009-0384-x-p</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">660</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Rezaei Behbehani, G.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">RETRACTED ARTICLE: Thermodynamic study on the interaction of cyanide ion and jack bean urease at different temperatures</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2009</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Akadémiai Kiadó, Budapest, Hungary 2009</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract A method based on Isothermal Titration Calorimety (ITC) is described for the thermodynamic assay of jack bean urease. Inhibitory activity of cyanide ion was examined against jack bean urease (JBU), at 27 and 37 oC in 30 mM Tris buffer of pH = 7. The binding parameters of the $ CN^{−} $ + JBU complexation have been calculated. It was found that in the low and high concentrations of the cyanide ions, the JBU structure was destabilized, resulting in a decrease in its biological activity.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Jack bean urease</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cyanide ion</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Isothermal titration calorimetry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Binding parameters</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Solvation model</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Saboury, A. 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Aug., Seite 1079-1083</subfield><subfield code="w">(DE-627)244148767</subfield><subfield code="w">(DE-600)1429493-X</subfield><subfield code="w">(DE-576)066397693</subfield><subfield code="x">1388-6150</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:100</subfield><subfield code="g">year:2009</subfield><subfield code="g">number:3</subfield><subfield code="g">day:28</subfield><subfield code="g">month:08</subfield><subfield code="g">pages:1079-1083</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">https://doi.org/10.1007/s10973-009-0384-x</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">100</subfield><subfield code="j">2009</subfield><subfield code="e">3</subfield><subfield code="b">28</subfield><subfield code="c">08</subfield><subfield code="h">1079-1083</subfield></datafield></record></collection>
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