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LA Moroz and NJ Gilmore
Fibrinolytic activity of normal plasma and blood has been measured by
125l-fibrin solid phase assay. Activity of plasma is not affected by
removal of plasminogenplasmin by affinity chromatography. Activities of
euglobulin and pseudoglobulin fractions are approximately equal.
epsilon-aminocaproic acid (EACA) (10 mM), tranexamic acid (10 mM),
diisopropylfluorophosphate (DFP, 50 mM), and soybean and lima bean trypsin
inhibitors (100 mug/ml) do not inhibit plasma activity at concentrations
that inhibit pure plasmin and urokinase-activated plasma. Activity is not
affected by glass contact and is not inhibited by inhibitors of contact or
enzymatic activation of Hageman factor (hexadimethrine bromide, 100 mug/ml;
cytochrome C, 250 mug/ml; spermidine, 2 mM; phenylmethylsulfonylfluoride, 1
mM). It is inhibited partially (30%-40%) by heating (56 degrees C, 30 min)
and by zymosan (2.5 mg/ml; 40%-90% inhibition), and is increased by
hydrazine (20 mM), salicylaldoxime (20 mM), DFP (50 mM), and
tosyl-L-arginine methyl ester (TAMe, 10 mM)-the latter two at
concentrations known to inhibit Cls of the classic, and factor D of the
alternate complement pathways. Increase fibrinolytic activity with TAMe is
associated with reciprocal decrease in classic and alternate complement
pathway activity. It is concluded that normal plasma fibrinolytic activity
is relatively independent of plasmin as the ultimate fibrinolytic enzyme,
that Hageman factor-dependent pathways are of minor importance, and that
significant heat-stable and heat-labile nonplasmin fibrinolytic activities
are operative. These may include proteinases involved in complement
activation, and in common control of classic and alternate complement
pathways, as well as other nonplasmin proteinases.
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| Copyright © 1976 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
