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plasmin
(redirected from plasmin inhibitors)

   Also found in: Dictionary/thesaurus, Encyclopedia, Wikipedia 0.01 sec.
plasmin /plas·min/ (plaz´min) an endopeptidase occurring in plasma as plasminogen, which is activated via cleavage by plasminogen activators; it solubilizes fibrin clots, degrades other coagulation-related proteins, and can be activated for use in therapeutic thrombolysis.
plas·min (plzmn)
n.
An enzyme that hydrolyzes peptides and esters of arginine and histidine and converts fibrin to soluble products. Also called fibrinase, fibrinolysin.

plasmin.
plasmin [plaz´min]
the active principle of the fibrinolytic or clot-lysing system, a proteolytic enzyme with a high specificity for fibrin and the particular ability to dissolve formed fibrin clots.

plasmin (plaz´min),
n collective term for one or more proteolytic enzymes found in the blood. The proteolytic enzymes are capable of digesting fibrin, fibrinogen, and proaccelerin. Plasminogen, the inactive form, may become active spontaneously in shed blood. An activator, fibrinokinase (fibrinolysokinase), is found in many animal tissues. Also called
fibrinolysin, lysin, plasma proteolytic enzyme, and
tryptase. See also plasminogen.

plasmin
the active principle of the fibrinolytic or clot-lysing system, a proteolytic enzyme formed from plasminogen which hydrolyzes fibrin, fibrinogen, factor V and other proteins. It has the particular ability to dissolve formed fibrin clots. Called also fibrinolysin.

plasmin inhibitors
include α2-macroglobulin, α1-antitrypsin, C1-inactivator, antithrombin III.

plasmin
A proteolytic enzyme formed from plasminogen that lyses blood clots; plasmin exists in free and bound–fibrin-adsorbed forms; the former is destroyed as it is formed by antiplasmins, the latter acts as a serine endopeptidase to solubilize fibrin clots; it hydrolyzes lysine and arginine bonds in certain proteins–eg, fibrinogen, coagulation factors V and VII. See tPA.


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Structure of an anti-plasmin inhibitor, eckol, isolated from the brown alga ecklonia kurome okamura and inhibitory activities of its derivatives on plasmin inhibitors.
The activity of this enzyme is controlled by certain inhibitors, such as plasmin inhibitors or inhibitors of plasminogen activators, that inhibit the activity of plasminogen activators so that plasminogen cannot be converted into plasmin.
Plasmin inhibitors are removed by acidification, and the unbound TPA is quantified by adding the sample to a mixture of PAI-deficient plasma containing plasminogen and a chromogenic substrate.
 
 
 
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