Effects of phosphoethanolamine and phosphoserine on blood coagulation mechanism

1959 ◽  
Vol 196 (5) ◽  
pp. 1020-1024
Author(s):  
J. L. Koppel ◽  
D. A. Mueller ◽  
L. V. Novak ◽  
J. H. Olwin
Keyword(s):  
Blood Coagulation ◽  
Human Blood ◽  
Brain Extract ◽  
Normal Human Plasma ◽  
Coagulation Mechanism ◽  
Normal Human ◽  
In Vitro Effects ◽  
Blood Coagulation Mechanism ◽  
Normal Human Blood

Phosphoethanolamine and phosphoserine were studied for their in vitro effects on various phases of the blood coagulation mechanism. When added to freshly drawn, normal human blood both substances exhibit marked anticoagulant characteristics. When added to normal human plasma in the presence of either brain extract thromboplastin or Russell viper venom they produce an inhibition of clot formation which becomes more pronounced with increasing concentration. The effects observed appear to be due to an interference with thrombin formation rather than to an inhibition of the thrombin fibrinogen reaction. Evidence has been obtained which suggests that, depending upon their concentration, phosphoethanolamine and phosphoserine may inhibit either the formation of a prothrombin-converting principle only or inhibit, in addition, the activity of this principle as well.

In Vitro Effects of the Acylated StreptokinasePlasminogen Activator Complex BRL 33 575 Incubated with Normal Human Plasma

1984 ◽  
Vol 51 (03) ◽  
pp. 403-405 ◽  
Author(s):  
B Lämmle ◽  
G Noll ◽  
T H Tran ◽  
A Lohri ◽  
F Duckert
Keyword(s):  
Human Plasma ◽  
Clinical Studies ◽  
Systemic Effects ◽  
In Vitro Experiments ◽  
Normal Human Plasma ◽  
Normal Human ◽  
Repeated Doses ◽  
In Vitro Effects ◽  
Activator Complex

SummaryThrombolysis with acylated streptokinase-plasminogen complexes is aimed to achieve fibrinolysis without systemic fibrinogenolysis. The p-aminobenzoyl-streptokinase-(Lys)-plasminogen-complex (BRL 33 575) should be particularly useful due to its slow deacylation rate. Unexpectedly, repeated doses of 10 mg of BRL 33 575 (corresponding to 310'000 streptokinase equivalent units) induced systemic effects in patients though less than streptokinase alone. In vitro incubation of normal human plasma with BRL 33 575 at concentrations used in patients resulted in nearly complete consumption of α2-antiplasmin and plasminogen and significant fibrinogenolysis within 3 hr. This demonstrates that - despite of slow deacylation of BRL 33 575 - the small amounts of activator generated are highly efficacious in activating plasma plasminogen under conditions in which no physiological clearance of the free activator takes place. Simulating the calculated activator release from BRL 33 575 by infusing equivalent amounts of streptokinase into plasma resulted in less pronounced effects. This is probably explained by anti-streptokinase antibodies which will neutralize the initially infused streptokinase but will be bound by BRL 33 575.Our in vitro experiments indicate that further clinical studies should be done with lower doses of BRL 33 575 or prolonged dosage intervals.

Defibrination of Normal Human Blood in Vitro: a Method giving a High Recovery of Untraumatized Cells

1977 ◽  
Vol 35 (4) ◽  
pp. 551-559 ◽  
Author(s):  
Penelope J. Bray ◽  
D. Ford ◽  
R. M. Gledhill ◽  
A. J. Grimes
Keyword(s):  
Human Blood ◽  
High Recovery ◽  
Normal Human ◽  
Normal Human Blood

Defibrination of Normal Human Blood for in vitro Cell Studies

Nature ◽  
1968 ◽  
Vol 218 (5137) ◽  
pp. 178-180 ◽  
Author(s):  
J. D. WILSON ◽  
A. J. GRIMES
Keyword(s):  
Human Blood ◽  
Normal Human ◽  
Normal Human Blood

Presence and Possible Origin of ɛ(γ-Glutamyl)Lysine Isodipeptide in Human Plasma

1992 ◽  
Vol 67 (01) ◽  
pp. 060-062 ◽  
Author(s):  
J Harsfalvi ◽  
E Tarcsa ◽  
M Udvardy ◽  
G Zajka ◽  
T Szarvas ◽  
...  
Keyword(s):  
Human Plasma ◽  
Fibrinolytic Therapy ◽  
Normal Human Plasma ◽  
Normal Human ◽  
Hplc Technique ◽  
Significant Change

Summaryɛ(γ-glutamyl)lysine isodipeptide has been detected in normal human plasma by a sensitive HPLC technique in a concentration of 1.9-3.6 μmol/1. Incubation of in vitro clotted plasma at 37° C for 12 h resulted in an increased amount of isodipeptide, and there was no further significant change when streptokinase was also present. Increased in vivo isodipeptide concentrations were also observed in hypercoagulable states and during fibrinolytic therapy.

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