The role of the Gla domain in the activation of bovine coagulation factor X by the snake venom protein XCP
The activation by XCP of coagulation factor X and a factor X species lacking the Gla-domain was studied in the presence and absence of Ca 2+. Both proteins could be activated at low rates in the absence of Ca 2+. The activation of the unmodified factor X was stimulated by the addition of Ca 2+, wher...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1983-02, Vol.111 (1), p.14-20 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Skogen, W.F. Bushong, D.S. Johnson, A.E. Cox, A.C. |
| description | The activation by XCP of coagulation factor X and a factor X species lacking the Gla-domain was studied in the presence and absence of Ca
2+. Both proteins could be activated at low rates in the absence of Ca
2+. The activation of the unmodified factor X was stimulated by the addition of Ca
2+, whereas GD factor X activation was insensitive to Ca
2+. The stimulatory effect of Ca
2+ seen with the unmodified factor X correlated strongly with a calcium-dependent change in intrinsic protein fluorescence. This conformational change required the Gla-domain as the fluorescence emission of GD factor X was the same with or without Ca
2+. Fluorescence changes which accompanied activation were the same for both factor X and GD factor X. This suggests that the Gla-domain does not participate in the structural changes which accompany activation. |
| doi_str_mv | 10.1016/S0006-291X(83)80110-7 |
| format | Article |
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2+. Both proteins could be activated at low rates in the absence of Ca
2+. The activation of the unmodified factor X was stimulated by the addition of Ca
2+, whereas GD factor X activation was insensitive to Ca
2+. The stimulatory effect of Ca
2+ seen with the unmodified factor X correlated strongly with a calcium-dependent change in intrinsic protein fluorescence. This conformational change required the Gla-domain as the fluorescence emission of GD factor X was the same with or without Ca
2+. Fluorescence changes which accompanied activation were the same for both factor X and GD factor X. This suggests that the Gla-domain does not participate in the structural changes which accompany activation.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(83)80110-7</identifier><identifier>PMID: 6830586</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>1-Carboxyglutamic Acid ; Animals ; Calcium - pharmacology ; Cattle ; coagulation factor X ; coagulation factor X activator ; Factor X - metabolism ; Factor Xa ; fluorescence ; Glutamates ; Kinetics ; Spectrometry, Fluorescence ; venom ; Viper Venoms - pharmacology ; Vipera russelli</subject><ispartof>Biochemical and biophysical research communications, 1983-02, Vol.111 (1), p.14-20</ispartof><rights>1983 Academic Press, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-f8d538a4377916aa8a3a0abf4fbeb5dd6df3016c22022205f5466102c5cf22023</citedby><cites>FETCH-LOGICAL-c457t-f8d538a4377916aa8a3a0abf4fbeb5dd6df3016c22022205f5466102c5cf22023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(83)80110-7$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6830586$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Skogen, W.F.</creatorcontrib><creatorcontrib>Bushong, D.S.</creatorcontrib><creatorcontrib>Johnson, A.E.</creatorcontrib><creatorcontrib>Cox, A.C.</creatorcontrib><title>The role of the Gla domain in the activation of bovine coagulation factor X by the snake venom protein XCP</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The activation by XCP of coagulation factor X and a factor X species lacking the Gla-domain was studied in the presence and absence of Ca
2+. Both proteins could be activated at low rates in the absence of Ca
2+. The activation of the unmodified factor X was stimulated by the addition of Ca
2+, whereas GD factor X activation was insensitive to Ca
2+. The stimulatory effect of Ca
2+ seen with the unmodified factor X correlated strongly with a calcium-dependent change in intrinsic protein fluorescence. This conformational change required the Gla-domain as the fluorescence emission of GD factor X was the same with or without Ca
2+. Fluorescence changes which accompanied activation were the same for both factor X and GD factor X. This suggests that the Gla-domain does not participate in the structural changes which accompany activation.</description><subject>1-Carboxyglutamic Acid</subject><subject>Animals</subject><subject>Calcium - pharmacology</subject><subject>Cattle</subject><subject>coagulation factor X</subject><subject>coagulation factor X activator</subject><subject>Factor X - metabolism</subject><subject>Factor Xa</subject><subject>fluorescence</subject><subject>Glutamates</subject><subject>Kinetics</subject><subject>Spectrometry, Fluorescence</subject><subject>venom</subject><subject>Viper Venoms - pharmacology</subject><subject>Vipera russelli</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1r3DAQhkVpSDdJf0JAp9IcnIwsS5ZPpSz5gkACSWBvQpZHrVLbSiXvQv595N0l14CEhpnnnUHzEnLK4JwBkxePACCLsmGrn4qfKWAMivoLWTBooCgZVF_J4gP5Ro5SeoEMVbI5JIdScRBKLsjL01-kMfRIg6NTjq97Q7swGD_SfOaMsZPfmMmHcWbasPEjUhvMn3W_y7pMhEhXtH3bCtJo_iHd4BgG-hrDhLnRavlwQg6c6RN-37_H5Pnq8ml5U9zdX98uf98VthL1VDjVCa5Mxeu6YdIYZbgB07rKtdiKrpOd4_n_tiyhzFc4UUnJoLTCujnHj8mPXd88-_8a06QHnyz2vRkxrJNWUEEpS_EpyLiQjZAyg2IH2hhSiuj0a_SDiW-agZ7N0Fsz9LxprbjemqHrrDvdD1i3A3Yfqv32c_3Xro55HRuPUSfrcbTY-Yh20l3wn0x4B0CImKk</recordid><startdate>19830228</startdate><enddate>19830228</enddate><creator>Skogen, W.F.</creator><creator>Bushong, D.S.</creator><creator>Johnson, A.E.</creator><creator>Cox, A.C.</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19830228</creationdate><title>The role of the Gla domain in the activation of bovine coagulation factor X by the snake venom protein XCP</title><author>Skogen, W.F. ; Bushong, D.S. ; Johnson, A.E. ; Cox, A.C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-f8d538a4377916aa8a3a0abf4fbeb5dd6df3016c22022205f5466102c5cf22023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>1-Carboxyglutamic Acid</topic><topic>Animals</topic><topic>Calcium - pharmacology</topic><topic>Cattle</topic><topic>coagulation factor X</topic><topic>coagulation factor X activator</topic><topic>Factor X - metabolism</topic><topic>Factor Xa</topic><topic>fluorescence</topic><topic>Glutamates</topic><topic>Kinetics</topic><topic>Spectrometry, Fluorescence</topic><topic>venom</topic><topic>Viper Venoms - pharmacology</topic><topic>Vipera russelli</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Skogen, W.F.</creatorcontrib><creatorcontrib>Bushong, D.S.</creatorcontrib><creatorcontrib>Johnson, A.E.</creatorcontrib><creatorcontrib>Cox, A.C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Skogen, W.F.</au><au>Bushong, D.S.</au><au>Johnson, A.E.</au><au>Cox, A.C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of the Gla domain in the activation of bovine coagulation factor X by the snake venom protein XCP</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1983-02-28</date><risdate>1983</risdate><volume>111</volume><issue>1</issue><spage>14</spage><epage>20</epage><pages>14-20</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The activation by XCP of coagulation factor X and a factor X species lacking the Gla-domain was studied in the presence and absence of Ca
2+. Both proteins could be activated at low rates in the absence of Ca
2+. The activation of the unmodified factor X was stimulated by the addition of Ca
2+, whereas GD factor X activation was insensitive to Ca
2+. The stimulatory effect of Ca
2+ seen with the unmodified factor X correlated strongly with a calcium-dependent change in intrinsic protein fluorescence. This conformational change required the Gla-domain as the fluorescence emission of GD factor X was the same with or without Ca
2+. Fluorescence changes which accompanied activation were the same for both factor X and GD factor X. This suggests that the Gla-domain does not participate in the structural changes which accompany activation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6830586</pmid><doi>10.1016/S0006-291X(83)80110-7</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1983-02, Vol.111 (1), p.14-20 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80402625 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 1-Carboxyglutamic Acid Animals Calcium - pharmacology Cattle coagulation factor X coagulation factor X activator Factor X - metabolism Factor Xa fluorescence Glutamates Kinetics Spectrometry, Fluorescence venom Viper Venoms - pharmacology Vipera russelli |
| title | The role of the Gla domain in the activation of bovine coagulation factor X by the snake venom protein XCP |
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