Alpha-2-plasmin inhibitor comprises a single domain
The reaction between plasmin and α 2PI (alpha-2-plasmin inhibitor), which constitutes a major regulatory step in fibrinolysis, involves both interactions between the kringle structures of plasmin and a complementary site on the inhibitor, and also between the inhibitor reactive center and the enzyme...
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Veröffentlicht in: | Biochemical and biophysical research communications 1986-09, Vol.139 (3), p.1062-1070 |
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container_title | Biochemical and biophysical research communications |
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creator | Magnotti, Ralph A. Halsall, H. Brian |
description | The reaction between plasmin and α
2PI (alpha-2-plasmin inhibitor), which constitutes a major regulatory step in fibrinolysis, involves both interactions between the kringle structures of plasmin and a complementary site on the inhibitor, and also between the inhibitor reactive center and the enzyme active site. An attempt was made to distinguish calorimetrically the two functional domains of α
2PI. Only one transition was seen, both in the DSC and UV experiments, contrary to the expected two. This transition was unaffected by K4 of plasminogen but was abolished in the presence of anhydrotrypsin. This suggests the major domain structure in α
2PI is associated with the reactive center. |
doi_str_mv | 10.1016/S0006-291X(86)80285-6 |
format | Article |
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2PI. Only one transition was seen, both in the DSC and UV experiments, contrary to the expected two. This transition was unaffected by K4 of plasminogen but was abolished in the presence of anhydrotrypsin. This suggests the major domain structure in α
2PI is associated with the reactive center.</description><subject>alpha-2-Antiplasmin - metabolism</subject><subject>Applied sciences</subject><subject>Binding Sites</subject><subject>Calorimetry, Differential Scanning</subject><subject>Exact sciences and technology</subject><subject>Fibrinolysin - metabolism</subject><subject>Fibrinolysis</subject><subject>Humans</subject><subject>Other techniques and industries</subject><subject>Ultraviolet Rays</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtKAzEUhoMotVYfoTALEV2MJjO5rqQUb1BwoYK7kEnOaGRuJlPBt3faDt26Oovz_efyITQn-Jpgwm9eMMY8zRR5v5T8SuJMspQfoCnBCqcZwfQQTffIMTqJ8QtjQihXEzTJFGWMqSnKF1X3adIs7SoTa98kvvn0he_bkNi27oKPEBOTRN98VJC4tja-OUVHpakinI11ht7u716Xj-nq-eFpuVilNpeqT4UDzpQjRQGYC6rKUlAggpSKARXOZERIpqywLndMFLZkLieSUcOsEi7D-Qxd7OZ2of1eQ-x17aOFqjINtOuohRhe5UoOINuBNrQxBij1cHhtwq8mWG9k6a0svTGhJddbWZoPufm4YF3U4Pap0c7QPx_7JlpTlcE01sc9JnOqhk8H7HaHwSDjx0PQ0XpoLDgfwPbatf6fQ_4AeYuFRA</recordid><startdate>19860930</startdate><enddate>19860930</enddate><creator>Magnotti, Ralph A.</creator><creator>Halsall, H. Brian</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><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>19860930</creationdate><title>Alpha-2-plasmin inhibitor comprises a single domain</title><author>Magnotti, Ralph A. ; Halsall, H. Brian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-7de659d1bbe06749ff74e171f95e47da217859c7cd3d57bcf5d31854a5c97d203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>alpha-2-Antiplasmin - metabolism</topic><topic>Applied sciences</topic><topic>Binding Sites</topic><topic>Calorimetry, Differential Scanning</topic><topic>Exact sciences and technology</topic><topic>Fibrinolysin - metabolism</topic><topic>Fibrinolysis</topic><topic>Humans</topic><topic>Other techniques and industries</topic><topic>Ultraviolet Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Magnotti, Ralph A.</creatorcontrib><creatorcontrib>Halsall, H. Brian</creatorcontrib><collection>Pascal-Francis</collection><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Magnotti, Ralph A.</au><au>Halsall, H. Brian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alpha-2-plasmin inhibitor comprises a single domain</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1986-09-30</date><risdate>1986</risdate><volume>139</volume><issue>3</issue><spage>1062</spage><epage>1070</epage><pages>1062-1070</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The reaction between plasmin and α
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2PI. Only one transition was seen, both in the DSC and UV experiments, contrary to the expected two. This transition was unaffected by K4 of plasminogen but was abolished in the presence of anhydrotrypsin. This suggests the major domain structure in α
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source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | alpha-2-Antiplasmin - metabolism Applied sciences Binding Sites Calorimetry, Differential Scanning Exact sciences and technology Fibrinolysin - metabolism Fibrinolysis Humans Other techniques and industries Ultraviolet Rays |
title | Alpha-2-plasmin inhibitor comprises a single domain |
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