Conformational changes of bovine β-trypsin and trypsinogen induced by divalent ions: An energy-dispersive X-ray diffraction and functional study
The radius of gyration ( R g) of bovine trypsinogen and β-trypsin was measured by an energy-dispersive X-ray technique as a function of Ca 2+ or SO 4 2− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca 2+ to its binding site(s) on both...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2006-05, Vol.449 (1), p.157-163 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Caracciolo, G. Martelli, A. Boumis, G. Bellelli, A. Caminiti, R. Congiu-Castellano, A. Amiconi, G. |
| description | The radius of gyration (
R
g) of bovine trypsinogen and β-trypsin was measured by an energy-dispersive X-ray technique as a function of Ca
2+ or SO
4
2− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca
2+ to its binding site(s) on both serine proteases and some of their adducts (with an effector and/or an inhibitor). As a whole, all information reported in the present work demonstrates that: (i) the strains exerted by different ions on these proteases produce diverse structural modifications; and (ii) at least in the case of Ca
2+, the changes in
R
g can be ascribed to the direct interaction of the binding site(s) on the protein matrix with the cation. |
| doi_str_mv | 10.1016/j.abb.2006.02.010 |
| format | Article |
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R
g) of bovine trypsinogen and β-trypsin was measured by an energy-dispersive X-ray technique as a function of Ca
2+ or SO
4
2− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca
2+ to its binding site(s) on both serine proteases and some of their adducts (with an effector and/or an inhibitor). As a whole, all information reported in the present work demonstrates that: (i) the strains exerted by different ions on these proteases produce diverse structural modifications; and (ii) at least in the case of Ca
2+, the changes in
R
g can be ascribed to the direct interaction of the binding site(s) on the protein matrix with the cation.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2006.02.010</identifier><identifier>PMID: 16549057</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Calcium - chemistry ; Cattle ; Ions ; Proteases ; Protein Conformation ; Protein Structure, Tertiary ; Radius of gyration ; Small angle scattering ; Structure ; Trypsin - analysis ; Trypsin - chemistry ; Trypsinogen ; Trypsinogen - analysis ; Trypsinogen - chemistry ; X-Ray Diffraction ; β-Trypsin</subject><ispartof>Archives of biochemistry and biophysics, 2006-05, Vol.449 (1), p.157-163</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c351t-e9a79f023f6826f9f277734235a2e02978b74aeaad75cbc32c73324074f2e7573</citedby><cites>FETCH-LOGICAL-c351t-e9a79f023f6826f9f277734235a2e02978b74aeaad75cbc32c73324074f2e7573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.abb.2006.02.010$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16549057$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Caracciolo, G.</creatorcontrib><creatorcontrib>Martelli, A.</creatorcontrib><creatorcontrib>Boumis, G.</creatorcontrib><creatorcontrib>Bellelli, A.</creatorcontrib><creatorcontrib>Caminiti, R.</creatorcontrib><creatorcontrib>Congiu-Castellano, A.</creatorcontrib><creatorcontrib>Amiconi, G.</creatorcontrib><title>Conformational changes of bovine β-trypsin and trypsinogen induced by divalent ions: An energy-dispersive X-ray diffraction and functional study</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The radius of gyration (
R
g) of bovine trypsinogen and β-trypsin was measured by an energy-dispersive X-ray technique as a function of Ca
2+ or SO
4
2− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca
2+ to its binding site(s) on both serine proteases and some of their adducts (with an effector and/or an inhibitor). As a whole, all information reported in the present work demonstrates that: (i) the strains exerted by different ions on these proteases produce diverse structural modifications; and (ii) at least in the case of Ca
2+, the changes in
R
g can be ascribed to the direct interaction of the binding site(s) on the protein matrix with the cation.</description><subject>Animals</subject><subject>Calcium - chemistry</subject><subject>Cattle</subject><subject>Ions</subject><subject>Proteases</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Radius of gyration</subject><subject>Small angle scattering</subject><subject>Structure</subject><subject>Trypsin - analysis</subject><subject>Trypsin - chemistry</subject><subject>Trypsinogen</subject><subject>Trypsinogen - analysis</subject><subject>Trypsinogen - chemistry</subject><subject>X-Ray Diffraction</subject><subject>β-Trypsin</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU2O1DAQRi0EYpqBA7BBXrFLKNtJHMNq1OJPGmk2jMTOcpxy41babuykpRxjrjIHmTORpiOxY1W1ePVKVR8hbxmUDFjzYV-aris5QFMCL4HBM7JhoJoCRFs9JxsAEIVqG3ZFXuW8B2CsavhLcsWaulJQyw152MbgYjqY0cdgBmp_mbDDTKOjXTz5gPTpsRjTfMw-UBN6uvZxh4H60E8We9rNtPcnM2AY6aLJH-lNoBgw7eai9_mIKfsT0p9FMmfSuWTsed9foZuCXZfncern1-SFM0PGN2u9JvdfPv_Yfitu775-397cFlbUbCxQGakccOGaljdOOS6lFBUXteEIXMm2k5VBY3pZ284KbqUQvAJZOY6yluKavL94jyn-njCP-uCzxWEwAeOUdSMVU61iC8guoE0x54ROH5M_mDRrBvqcg97rJQd9zkED10sOy8y7VT51B-z_TayPX4BPFwCXE08ek87WY1i-6RPaUffR_0f_Bxezm6E</recordid><startdate>20060515</startdate><enddate>20060515</enddate><creator>Caracciolo, G.</creator><creator>Martelli, A.</creator><creator>Boumis, G.</creator><creator>Bellelli, A.</creator><creator>Caminiti, R.</creator><creator>Congiu-Castellano, A.</creator><creator>Amiconi, 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>20060515</creationdate><title>Conformational changes of bovine β-trypsin and trypsinogen induced by divalent ions: An energy-dispersive X-ray diffraction and functional study</title><author>Caracciolo, G. ; Martelli, A. ; Boumis, G. ; Bellelli, A. ; Caminiti, R. ; Congiu-Castellano, A. ; Amiconi, G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-e9a79f023f6826f9f277734235a2e02978b74aeaad75cbc32c73324074f2e7573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Calcium - chemistry</topic><topic>Cattle</topic><topic>Ions</topic><topic>Proteases</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>Radius of gyration</topic><topic>Small angle scattering</topic><topic>Structure</topic><topic>Trypsin - analysis</topic><topic>Trypsin - chemistry</topic><topic>Trypsinogen</topic><topic>Trypsinogen - analysis</topic><topic>Trypsinogen - chemistry</topic><topic>X-Ray Diffraction</topic><topic>β-Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Caracciolo, G.</creatorcontrib><creatorcontrib>Martelli, A.</creatorcontrib><creatorcontrib>Boumis, G.</creatorcontrib><creatorcontrib>Bellelli, A.</creatorcontrib><creatorcontrib>Caminiti, R.</creatorcontrib><creatorcontrib>Congiu-Castellano, A.</creatorcontrib><creatorcontrib>Amiconi, 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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Caracciolo, G.</au><au>Martelli, A.</au><au>Boumis, G.</au><au>Bellelli, A.</au><au>Caminiti, R.</au><au>Congiu-Castellano, A.</au><au>Amiconi, G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformational changes of bovine β-trypsin and trypsinogen induced by divalent ions: An energy-dispersive X-ray diffraction and functional study</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2006-05-15</date><risdate>2006</risdate><volume>449</volume><issue>1</issue><spage>157</spage><epage>163</epage><pages>157-163</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The radius of gyration (
R
g) of bovine trypsinogen and β-trypsin was measured by an energy-dispersive X-ray technique as a function of Ca
2+ or SO
4
2− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca
2+ to its binding site(s) on both serine proteases and some of their adducts (with an effector and/or an inhibitor). As a whole, all information reported in the present work demonstrates that: (i) the strains exerted by different ions on these proteases produce diverse structural modifications; and (ii) at least in the case of Ca
2+, the changes in
R
g can be ascribed to the direct interaction of the binding site(s) on the protein matrix with the cation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16549057</pmid><doi>10.1016/j.abb.2006.02.010</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 2006-05, Vol.449 (1), p.157-163 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Calcium - chemistry Cattle Ions Proteases Protein Conformation Protein Structure, Tertiary Radius of gyration Small angle scattering Structure Trypsin - analysis Trypsin - chemistry Trypsinogen Trypsinogen - analysis Trypsinogen - chemistry X-Ray Diffraction β-Trypsin |
| title | Conformational changes of bovine β-trypsin and trypsinogen induced by divalent ions: An energy-dispersive X-ray diffraction and functional study |
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