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1.
Eksp Klin Farmakol ; 71(4): 30-4, 2008.
Article in Russian | MEDLINE | ID: mdl-18819438

ABSTRACT

We have studied in vitro the ability of the Siberian cedar crust (SCC) extract (Pinus sibirica Du Tour) and arabinogalactan sulphate (AGS) extracted from wood of Siberiam pine-tree (Larix sibirica Ledeb.) to increase the human blood plasma coagulation time and also to inhibit the amydolytic activity of thrombin (aIIa) and the coagulation factor Xa (aXa). A method has been developed by means of which SCC increases the aXa activity by a factor of 3.7 and the aIIà activity by a factor of 2.5. The AGS preparation increased the blood plasma coagulation time in the test for activated partial thromboplastin time. An effective concentration, at which the time of plasma coagulation was increased by a factor of 2 (in comparison to the control) was 2.94 +/- 0.33 mg/ml. AGS did not exhibit the ability to inhibit the Xa activity.


Subject(s)
Anticoagulants/pharmacology , Blood Coagulation/drug effects , Cedrus/chemistry , Galactans/pharmacology , Plant Extracts/pharmacology , Factor Xa Inhibitors , Humans , In Vitro Techniques , Plant Bark/chemistry , Thrombin/antagonists & inhibitors
3.
Biull Eksp Biol Med ; 96(9): 42-5, 1983 Sep.
Article in Russian | MEDLINE | ID: mdl-6311310

ABSTRACT

The cAMP-dependent phosphorylation of proteins of both non-fractionated microsomes of the dog myocardium and phospholamban were studied in experimental myocardial infarction. In the presence of cAMP and exogenous protein kinase, the incorporation of 33P into microsomes and phospholamban of the affected muscle decreased as compared to that in the intact heart muscle. During infarction, partial degradation of phospholamban was observed. At the same time there was an increase in endogenous proteinase activity in microsomes of the affected muscle. The phosphorylation of phospholamban combined with its treatment by trypsin was investigated. The data indicate the correlation between the degree of phospholamban phosphorylation and its proteinase resistance in both the affected and intact myocardium.


Subject(s)
Calcium-Binding Proteins/metabolism , Endopeptidases/metabolism , Myocardial Infarction/metabolism , Protein Kinases/metabolism , Animals , Cyclic AMP/metabolism , Dogs , Microsomes/enzymology , Phosphorylation
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