Zobrazeno 1 - 10
of 496
pro vyhledávání: '"JH Griffin"'
Autor:
A Gruber, JH Griffin
Publikováno v:
Blood. 79:2340-2348
The antithrombotic enzyme, activated protein C (APC) was measured in blood using an enzyme capture assay (ECA). The ECA involved (1) collection of blood into anticoagulant containing a reversible inhibitor of the enzyme, (2) specific affinity capture
Publikováno v:
Europe PubMed Central
Three dimensional homology models for the C1 and C2 domains of factor VIII (FVIII) were generated. Each C domain formed a beta-sandwich, and C1 was covalently connected to C2 in a head-to-head orientation. Of the250 missense mutations that cause FVII
Publikováno v:
Europe PubMed Central
An important risk factor for thrombosis is the polymorphism R506Q in factor V that causes resistance of factor Va to proteolytic inactivation by activated protein C (APC). To study the potential influence of the carbohydrate moieties of factor Va on
Autor:
Martine Aiach, JH Griffin, Brigitte Jude, Martine Alhenc-Gelas, JF Abgrall, JS Greengard, Sophie Gandrille, Irène Juhan-Vague
Publikováno v:
Blood. 86(1)
Because multiple risk factors in one patient may increase the clinical expression of thrombophilia, we assessed the presence in protein C- deficient patients of the factor V Arg 506 Gln mutation responsible for activated protein C resistance. Using a
Publikováno v:
Blood. 79(12)
The levels of total, free, and bound protein S and C4BP were determined using enzyme-linked immunosorbent assays (ELISAs) in plasma samples (8 males and 8 females) that were individually subjected to immunoadsorption studies in which “free protein
Publikováno v:
Blood. 77(8)
In vivo complex formation of activated protein C with protein C inhibitor (APC-PCI) and with alpha 1-antitrypsin (APC-alpha 1AT) following infusion of 0.25 or 1.0 mg APC/kg in 1 hour into baboons was studied using immunoblotting and sandwich enzyme-l
Publikováno v:
Blood. 63:486-489
Purified human factor VIII procoagulant protein (VIII:C) was treated with purified human activated protein C (APC) and the loss of VIII:C activity correlated with proteolysis of the VIII:C polypeptides. APC proteolyzed all VIII:C polypeptides with mo
Autor:
PN Walsh, JH Griffin
Publikováno v:
Blood. 57:106-118
Autor:
G Tans, JH Griffin
Publikováno v:
Blood. 59:69-75
Incubation of normal human plasma with low amounts of sulfatides resulted in the initiation of intrinsic coagulation and the appearance of kallikrein activity. The optimal initiation of procoagulant and kallikrein amidolytic activity was dependent on
Publikováno v:
Blood. 74:173-181
This study investigates the role of the gamma-carboxyglutamic acid (gla) containing domain of activated protein C in interactions with both platelet-derived and purified type 1 plasminogen activator inhibitor (PAI-1). The activity of human platelet P