Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P10
The following peptide was synthesized by classical methods in solution: Ac-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-Arg-Val-NHCH3 (F-8). The Michaelis-Menten parameters for the hydrolysis of the Arg-Gly bond in F-8 by thrombin were determined to be Kcat = 31 X 10(-11) M [(NIH unit/L) s]-1 and...
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| Veröffentlicht in: | Biochemistry (Easton) 1983-08, Vol.22 (18), p.4170-4174 |
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| container_end_page | 4174 |
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| container_issue | 18 |
| container_start_page | 4170 |
| container_title | Biochemistry (Easton) |
| container_volume | 22 |
| creator | Marsh, Henry C Meinwald, Yvonne C Thannhauser, Theodore W Scheraga, Harold A |
| description | The following peptide was synthesized by classical methods in solution: Ac-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-Arg-Val-NHCH3 (F-8). The Michaelis-Menten parameters for the hydrolysis of the Arg-Gly bond in F-8 by thrombin were determined to be Kcat = 31 X 10(-11) M [(NIH unit/L) s]-1 and KM = 310 X 10(-6) M. Comparison of these values with those determined previously for native fibrinogen and for a series of similar synthetic peptides, together with information about the amino acid sequences of this portion of the A alpha chain of abnormal fibrinogens, suggests an important role for Asp at position P10. Differences in the Michaelis-Menten parameters between F-8 and the 51-residue N-terminal CNBr fragment of the A alpha chain of fibrinogen correspond to only 1-2 kcal/mol in binding affinity. |
| doi_str_mv | 10.1021/bi00287a002 |
| format | Article |
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Kinetic evidence for involvement of aspartic acid at position P10</title><source>MEDLINE</source><source>American Chemical Society Journals</source><creator>Marsh, Henry C ; Meinwald, Yvonne C ; Thannhauser, Theodore W ; Scheraga, Harold A</creator><creatorcontrib>Marsh, Henry C ; Meinwald, Yvonne C ; Thannhauser, Theodore W ; Scheraga, Harold A</creatorcontrib><description>The following peptide was synthesized by classical methods in solution: Ac-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-Arg-Val-NHCH3 (F-8). The Michaelis-Menten parameters for the hydrolysis of the Arg-Gly bond in F-8 by thrombin were determined to be Kcat = 31 X 10(-11) M [(NIH unit/L) s]-1 and KM = 310 X 10(-6) M. Comparison of these values with those determined previously for native fibrinogen and for a series of similar synthetic peptides, together with information about the amino acid sequences of this portion of the A alpha chain of abnormal fibrinogens, suggests an important role for Asp at position P10. Differences in the Michaelis-Menten parameters between F-8 and the 51-residue N-terminal CNBr fragment of the A alpha chain of fibrinogen correspond to only 1-2 kcal/mol in binding affinity.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00287a002</identifier><identifier>PMID: 6626500</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Animals ; Aspartic Acid ; Biological and medical sciences ; Blood coagulation. Blood cells ; Cattle ; Coagulation factors ; Fibrinogen - metabolism ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Magnetic Resonance Spectroscopy ; Molecular and cellular biology ; Oligopeptides - chemical synthesis ; Protein Conformation ; Substrate Specificity ; Thrombin - metabolism</subject><ispartof>Biochemistry (Easton), 1983-08, Vol.22 (18), p.4170-4174</ispartof><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a364t-2d20c24adf350be09855fd056cdeb90633ac9f1323bcb2a3605d70183b0ccaab3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00287a002$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00287a002$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9364582$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6626500$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marsh, Henry C</creatorcontrib><creatorcontrib>Meinwald, Yvonne C</creatorcontrib><creatorcontrib>Thannhauser, Theodore W</creatorcontrib><creatorcontrib>Scheraga, Harold A</creatorcontrib><title>Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P10</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The following peptide was synthesized by classical methods in solution: Ac-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-Arg-Val-NHCH3 (F-8). The Michaelis-Menten parameters for the hydrolysis of the Arg-Gly bond in F-8 by thrombin were determined to be Kcat = 31 X 10(-11) M [(NIH unit/L) s]-1 and KM = 310 X 10(-6) M. Comparison of these values with those determined previously for native fibrinogen and for a series of similar synthetic peptides, together with information about the amino acid sequences of this portion of the A alpha chain of abnormal fibrinogens, suggests an important role for Asp at position P10. Differences in the Michaelis-Menten parameters between F-8 and the 51-residue N-terminal CNBr fragment of the A alpha chain of fibrinogen correspond to only 1-2 kcal/mol in binding affinity.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Aspartic Acid</subject><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>Cattle</subject><subject>Coagulation factors</subject><subject>Fibrinogen - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular and cellular biology</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Protein Conformation</subject><subject>Substrate Specificity</subject><subject>Thrombin - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkEFvFCEYhonR1LV68mzCwejBTP0GBmY4No21xqpV68UL-WAYS52BEWY3-u9lu5uNBy_wkffhCbyEPK3hpAZWvzYegHUtlvUeWdWCQdUoJe6TFQDIiikJD8mjnG_LsYG2OSJHUjIpAFZk_uDsDQafJxoHinbxMWyn5SbFyfgyBzp4k3yIP1w4oe99cIu31G1874J1dIiJ-rCJ48ZNLix3ljxj2kJofU9xoXPM_k58VcNj8mDAMbsn-_2YfDt_c312UV1-evvu7PSyQi6bpWI9A8sa7AcuwDhQnRBDD0La3hkFknO0aqg548YaVu6A6FuoO27AWkTDj8mLnXdO8dfa5UVPPls3jhhcXGfdgVSNAlXAVzvQpphzcoOek58w_dE16G2_-p9-C_1sr12byfUHdl9oyZ_vc8wWxyFhsD4fMFU-J7qtptphPi_u9yHG9FPLlrdCX1991V--X3SfP55z3RX-5Y5Hm_VtXKdQuvvvA_8C3WeeRg</recordid><startdate>19830801</startdate><enddate>19830801</enddate><creator>Marsh, Henry C</creator><creator>Meinwald, Yvonne C</creator><creator>Thannhauser, Theodore W</creator><creator>Scheraga, Harold A</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>19830801</creationdate><title>Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P10</title><author>Marsh, Henry C ; Meinwald, Yvonne C ; Thannhauser, Theodore W ; Scheraga, Harold A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a364t-2d20c24adf350be09855fd056cdeb90633ac9f1323bcb2a3605d70183b0ccaab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Aspartic Acid</topic><topic>Biological and medical sciences</topic><topic>Blood coagulation. Blood cells</topic><topic>Cattle</topic><topic>Coagulation factors</topic><topic>Fibrinogen - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Molecular and cellular biology</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Protein Conformation</topic><topic>Substrate Specificity</topic><topic>Thrombin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marsh, Henry C</creatorcontrib><creatorcontrib>Meinwald, Yvonne C</creatorcontrib><creatorcontrib>Thannhauser, Theodore W</creatorcontrib><creatorcontrib>Scheraga, Harold A</creatorcontrib><collection>Istex</collection><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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marsh, Henry C</au><au>Meinwald, Yvonne C</au><au>Thannhauser, Theodore W</au><au>Scheraga, Harold A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P10</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1983-08-01</date><risdate>1983</risdate><volume>22</volume><issue>18</issue><spage>4170</spage><epage>4174</epage><pages>4170-4174</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The following peptide was synthesized by classical methods in solution: Ac-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-Arg-Val-NHCH3 (F-8). The Michaelis-Menten parameters for the hydrolysis of the Arg-Gly bond in F-8 by thrombin were determined to be Kcat = 31 X 10(-11) M [(NIH unit/L) s]-1 and KM = 310 X 10(-6) M. Comparison of these values with those determined previously for native fibrinogen and for a series of similar synthetic peptides, together with information about the amino acid sequences of this portion of the A alpha chain of abnormal fibrinogens, suggests an important role for Asp at position P10. Differences in the Michaelis-Menten parameters between F-8 and the 51-residue N-terminal CNBr fragment of the A alpha chain of fibrinogen correspond to only 1-2 kcal/mol in binding affinity.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>6626500</pmid><doi>10.1021/bi00287a002</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemistry (Easton), 1983-08, Vol.22 (18), p.4170-4174 |
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| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Amino Acid Sequence Animals Aspartic Acid Biological and medical sciences Blood coagulation. Blood cells Cattle Coagulation factors Fibrinogen - metabolism Fundamental and applied biological sciences. Psychology Kinetics Magnetic Resonance Spectroscopy Molecular and cellular biology Oligopeptides - chemical synthesis Protein Conformation Substrate Specificity Thrombin - metabolism |
| title | Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P10 |
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