Isolation and Properties of a Low Molecular Weight Antiplasmin of Human Blood Platelets and Serum

Mui, P. T. K.; James, Harold L.; Ganguly, P.

doi:10.1111/j.1365-2141.1975.tb02749.x

Cited by 28 publications

(6 citation statements)

References 24 publications

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“…In addition to these observations, plasma inhibitors of fibrinolysis which possess properties similar to those ofa2-PI were recently described (31)(32)(33)(34)(35). The question as to whether or not a2-PI is identical with any one of these inhibitors needs further investigation, including elucidation of the physicochemical and immunochemical properties of each inhibitor.…”

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confidence: 99%

The behavior of alpha2-plasmin inhibitor in fibrinolytic states.

Aoki¹,

Moroi²,

Matsuda³

et al. 1977

J. Clin. Invest.

167

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A B S T R A C T Human plasma a2-plasmin inhibitor in fibrinolytic states was studied using immunochemical methods and radioiodinated plasminogen. The concentration and activity of plasma a2-plasmin inhibitor decreased when urokinase was added to plasma in vitro or infused intravenously in man. The decrease was associated with the appearance of plasmin-a2-plasmin inhibitor complex which subsequently disappeared from the circulation in a short time. A decrease of other major inhibitors, such as a2-macroglobulin and a1-antitrypsin, was not observed when the amount of urokinase added or infused was relatively small, and conversion of plasminogen to plasmin was not extensive. The formation of plasmina2-macroglobulin complex was observed only when plasma plasminogen was activated with a larger amount of urokinase, and after most of the a2-plasmin inhibitor was consumed by forming complexes with plasmin. The formation of plasmin-al-antitrypsin complex was not observed even in the highly activated plasma unless exogenous plasmin was added to the plasma. a2-Plasmin inhibitor was the only inhibitor of which the concentration in plasma was significantly decreased in patients with disseminated intravascular coagulation and fibrinolysis among the major plasmin inhibitors in plasma. The most reactive inhibitor for regulating plasma fibrinolysis very likely is a2-plasmin inhibitor.

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mentioning

confidence: 99%

The behavior of alpha2-plasmin inhibitor in fibrinolytic states.

Aoki¹,

Moroi²,

Matsuda³

et al. 1977

J. Clin. Invest.

167

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“…50000. Previously published molecular masses of platelet anti-fibrinolytic activity are less than 100000 (Mui et al, 1975), 30000 (Joist et al, 1976), 35000 (Ganguly, 1972), 40000 (Wakabayashi et al, 1970, 45000 (Murray et al, 1974), 70000 (Moore et al, 1975) and over 110000 (McDonagh et al, 1969). Whether the present inhibitor is identical with one or more of these inhibitors is difficult to resolve, since no data are available on the rate of inhibition of plasmin, the complex-formation with plasmin, the possible affinity for plasminogen or the dissociation constant for the inhibitor-plasmin complex.…”

Section: Coopermentioning

confidence: 95%

Partial purification and characterization of a new fast-acting plasmin inhibitor from human platelets. Evidence for non-identity with the known plasma proteinase inhibitors

Hansen¹,

Clemmensen²

1980

Biochemical Journal

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An inhibitor of the plasma proteinase plasmin (EC 3.4.21.7) was partially purified from washed and lysed human blood platelets by (NH4)2SO4 fractionation and affinity chromatrography on Sepharose-linked purified plasminogen. The material contained none of the known plasma proteinase inhibitors when studied by crossed-immunoelectrophoresis and electroimmunoassay, but inhibited a clot-lysis-time assay and an esterolytic assay that used the synthetic substrate S-2251 (D-Val-Leu-Lys-p-nitroanilide). The inhibitory activity had the same mobility as the alpha 2-plasma proteins on preparative agarose-gel electrophoresis. Titration of the inhibitor preparation by active-site-titrated plasmin demonstrated a dissociation constant of approx. 0.1 nM. The inhibition was complete within 1 min. The inhibitor increased the mobility in agarose-gel electrophoresis of purified activator-free plasmin or 125I-labelled plasmin, as demonstrated by crossed-immunoelectrophoresis against specific immunoglobulins against plasminogen or by radioautography. The results strongly suggest the presence in platelets of a plasmin inhibitor different from the known plasma proteinase inhibitors.

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“…The plasma concentration of α2-PI is 0.7 ± 0.06 mg/L. α2-PI is also present in platelet α-granules at low concentrations and constitutes only 0.05% of α2-PI present in whole blood [26]. Its half-life is 2.6…”

Section: α2-plasmin Inhibitor Deficiencymentioning

confidence: 98%