Results 251 to 260 of about 151,729 (305)
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Blood Coagulation & Fibrinolysis, 1992
Plasminogen is the zymogen form of plasmin, a broad specificity serine protease whose activity contributes to a variety of normal and pathological conditions, including intravascular thrombolysis and extracellular proteolysis. Plasminogen contains seven structural units or 'domains', each of which confer specific properties on the molecule. The kringle
C P, Ponting +2 more
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Plasminogen is the zymogen form of plasmin, a broad specificity serine protease whose activity contributes to a variety of normal and pathological conditions, including intravascular thrombolysis and extracellular proteolysis. Plasminogen contains seven structural units or 'domains', each of which confer specific properties on the molecule. The kringle
C P, Ponting +2 more
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Journal of Thrombosis and Haemostasis, 2007
Plasminogen (plg) deficiency has been classified as (i) hypoplasminogenemia or 'true' type I plg deficiency, and (ii) dysplasminogenemia, also called type II plg deficiency. Both forms, severe hypoplasminogenemia and dysplasminogenemia, are not causally linked to venous thrombosis.
V, Schuster, B, Hügle, K, Tefs
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Plasminogen (plg) deficiency has been classified as (i) hypoplasminogenemia or 'true' type I plg deficiency, and (ii) dysplasminogenemia, also called type II plg deficiency. Both forms, severe hypoplasminogenemia and dysplasminogenemia, are not causally linked to venous thrombosis.
V, Schuster, B, Hügle, K, Tefs
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The binding of plasminogen to fibrin: Evidence for plasminogen-bridging
Thrombosis Research, 1982The ability of plasminogen to cause precipitation of soluble fibrin oligomers has been observed and certain features of the phenomenon investigated. The process is mediated by the lysine-binding sites and it appears that at least two such sites are required.
A J, Garman, R A, Smith
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Mechanisms of Plasminogen Activation by Mammalian Plasminogen Activators
Enzyme, 2017Plasminogen activators convert the proenzyme plasminogen to the active serine protease plasmin by hydrolysis of the Arg^560-Val^561 peptide bond. Physiological plasminogen activation is however regulated by several additional molecular interactions resulting in fibrin-specific clot lysis.
H R, Lijnen, D, Collen
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Plasminogen activators and plasminogen activator inhibitors in endometriosis
Frontiers in Bioscience, 2005Endometriosis is one of the most frequent benign gynecological diseases that affect women. Little is known about the pathogenesis and etiology of endometriosis, despite the numerous studies performed in this field. Although endometriosis is a benign disease, the endometrial tissue, after attachment to the peritoneum, has the ability to grow and invade ...
Juan, Gilabert-Estelles +6 more
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Studies on the kinetics of plasminogen activation by tissue plasminogen activator
BBA - Proteins and Proteomics, 1982The steady-state rate of plasminogen activation by tissue plasminogen activator has been determined at various plasminogen concentrations. A plasmin substrate method similar to that presented by Christensen and Müllertz (Biochim. Biophys. Acta 480 (1977) 257-281) was used.
Mats Rånby, M Rånby
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Thrombosis Research, 1988
Glu-plasminogen (Glu-plg), Lys-plg and Val442-plg (mini-plg) were activated by urokinase (UK), streptokinase (SK) or tissue plasminogen activator (t-PA). Their activation rates were kinetically analyzed. UK activated Lys-plg with smaller Km and nearly identical Vmax as Glu-plg.
A, Takada, Y, Takada, Y, Sugawara
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Glu-plasminogen (Glu-plg), Lys-plg and Val442-plg (mini-plg) were activated by urokinase (UK), streptokinase (SK) or tissue plasminogen activator (t-PA). Their activation rates were kinetically analyzed. UK activated Lys-plg with smaller Km and nearly identical Vmax as Glu-plg.
A, Takada, Y, Takada, Y, Sugawara
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Thrombosis Research, 1984
The potentiating effect of fibrin monomer on plasminogen activation by tissue-type plasminogen activator is much more important with lys-plasminogen than with mini-plasminogen (which lacks the high affinity lysine-binding site important for binding to fibrin).
F W, Dunn +6 more
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The potentiating effect of fibrin monomer on plasminogen activation by tissue-type plasminogen activator is much more important with lys-plasminogen than with mini-plasminogen (which lacks the high affinity lysine-binding site important for binding to fibrin).
F W, Dunn +6 more
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Biochemistry, 1994
The conformations of Glu-plasminogen and defined proteolytic fragments, in the presence and absence of 6-aminohexanoic acid (6-AHA), trans-4-(aminomethyl)cyclohexanecarboxylic acid (t-AMCHA), and benzamidine, were studied using three methods: size-exclusion high-performance liquid chromatography (SE-HPLC), small-angle X-ray scattering (SAXS), and ...
J M, Marshall, A J, Brown, C P, Ponting
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The conformations of Glu-plasminogen and defined proteolytic fragments, in the presence and absence of 6-aminohexanoic acid (6-AHA), trans-4-(aminomethyl)cyclohexanecarboxylic acid (t-AMCHA), and benzamidine, were studied using three methods: size-exclusion high-performance liquid chromatography (SE-HPLC), small-angle X-ray scattering (SAXS), and ...
J M, Marshall, A J, Brown, C P, Ponting
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Activation of Bovine Plasminogen by the Plasminogen Activator in Animal Tissue
Thrombosis and Haemostasis, 1960Summary1. The activation of bovine plasminogen by means of the plasminogen activator from pig heart tissue has been studied on heated fibrin and on casein.2. Small, but varying, amounts of activator can be extracted from crude activator powder during the experiment and interfere therefore with estimations on normal, plasminogen containing fibrin.3. The
T, ABE, T, ASTRUP
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