Document Detail


Kinetic behavior of the multienzyme system of blood prostanoid synthesis.
MedLine Citation:
PMID:  3013337     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A kinetic scheme of the prostacyclin-thromboxane system has been evolved on the basis of our own experimental material and the results described elsewhere. The kinetic behavior of the model has been analysed with the aid of computer technology by varying the following parameters: phospholipase activities, free arachidonic acid exchange rates between platelets and endothelium, prostaglandin H (PGH) synthetase biosynthesis rates, velocities of arachidonic acid pathways other than cyclooxygenase ones. It has been demonstrated that the biological system is capable of sustaining prostacyclin and thromboxane concentrations at steady fixed levels within a wide range of kinetic parameters.
Authors:
S D Varfolomeev; V P Gachok; A T Mevkh
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Bio Systems     Volume:  19     ISSN:  0303-2647     ISO Abbreviation:  BioSystems     Publication Date:  1986  
Date Detail:
Created Date:  1986-07-29     Completed Date:  1986-07-29     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0430773     Medline TA:  Biosystems     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  45-54     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Arachidonic Acid
Arachidonic Acids / blood
Blood Platelets / metabolism
Endothelium / metabolism
Epoprostenol / biosynthesis*,  blood
Humans
Kinetics
Mathematics
Models, Biological*
Multienzyme Complexes / biosynthesis*,  blood
Phospholipases / blood
Phosphoric Diester Hydrolases / blood
Prostaglandin-Endoperoxide Synthases / biosynthesis,  blood
Prostaglandins / biosynthesis,  blood
Thromboxanes / biosynthesis*,  blood
Chemical
Reg. No./Substance:
0/Arachidonic Acids; 0/Multienzyme Complexes; 0/Prostaglandins; 0/Thromboxanes; 35121-78-9/Epoprostenol; 506-32-1/Arachidonic Acid; EC 1.14.99.1/Prostaglandin-Endoperoxide Synthases; EC 3.1.-/Phospholipases; EC 3.1.4.-/Phosphoric Diester Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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