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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
1984-12-27
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pubmed:abstractText |
The kinetics of the thrombin-induced release of fibrinopeptides from several variants of human fibrinogen, and from the plasmin digestion fragment E thereof, have been studied by using an HPLC technique to separate the reaction products. The data were analyzed in terms of a Michaelis-Menten mechanism in which the A alpha and B beta chains compete for thrombin. Phosphorylation of Ser-3 of the A alpha chain appears to increase the rate of release of the corresponding phosphorylated peptide A from fibrinogen, due to enhanced binding of thrombin (lower value of the Michaelis-Menten constant KM). However, phosphorylation does not affect the rate of release of the unphosphorylated A or B peptides. Increase in the length of the gamma chain (at the C-terminus) does not affect the rate of release of any of the fibrinopeptides. The rate of release of the A peptide from fragment E (which is devoid of the B peptide) is similar to that for the complete fibrinogen molecule. These results are in agreement with an earlier conclusion [Martinelli, R. A., & Scheraga, H. A. (1980) Biochemistry 19, 2343] that the A alpha and B beta chains behave independently in their competition for thrombin; i.e., the hydrolyzable Arg-Gly bonds of the A alpha and B beta chains are both accessible to thrombin.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fibrin Fibrinogen Degradation...,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinolysin,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinopeptide A,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinopeptide B,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/fibrinogen fragment E
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4681-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6238619-Fibrin Fibrinogen Degradation Products,
pubmed-meshheading:6238619-Fibrinogen,
pubmed-meshheading:6238619-Fibrinolysin,
pubmed-meshheading:6238619-Fibrinopeptide A,
pubmed-meshheading:6238619-Fibrinopeptide B,
pubmed-meshheading:6238619-Humans,
pubmed-meshheading:6238619-Kinetics,
pubmed-meshheading:6238619-Macromolecular Substances,
pubmed-meshheading:6238619-Mathematics,
pubmed-meshheading:6238619-Phosphorylation
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pubmed:year |
1984
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pubmed:articleTitle |
Comparison of structures of various human fibrinogens and a derivative thereof by a study of the kinetics of release of fibrinopeptides.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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