Enzyme studies on human blood; interrelation of heparin and fibrinogen fractions.

نویسنده

  • G Y SHINOWARA
چکیده

I NVESTIGATIONS on the possible mechanism of the anticoagulant action of heparin have centered largely on the problem of its cofactor. In 1918, Howell and Holt (I) showed that heparin requires a blood factor to prevent the coagulation of fibrinogen by thrombin. Subsequently Quick (2) suggested that an albumin fraction contains normal antithrombin, which together with heparin, exerts a powerful anticoagulant action. Others (3,4, 5) confirmed that the heparin cofactor is a substance associated with an albumin fraction, but not crystalline albumin. In a previous communication from this laboratory (6) it was demonstrated that human plasma albumin actually accelerates the reaction of fibrinogen fractions with thrombin. Therefore, in view of this nnding and the reported synergism of antithrombin and heparin, experiments on the influence of heparin on fibrinogen fractions were undertaken.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Heparin-induced release of extracellular superoxide dismutase to human blood plasma.

Extracellular superoxide dismutase (SOD) has previously been shown to be the major SOD isoenzyme in extracellular fluids. Upon chromatography on heparin-Sepharose it was separated into three fractions: A, without affinity; B, with intermediate affinity; and C, with relatively strong heparin affinity. Intravenous injection of heparin leads to a prompt increase in plasma extracellular-superoxide-...

متن کامل

Human mast cell tryptase fibrinogenolysis: kinetics, anticoagulation mechanism, and cell adhesion disruption.

Tryptase is a 31 kDa, glycosylated, trypsin-like enzyme stored in and released from mast cell granules. Human tryptase exists as a tetramer, binds heparin, and has a limited substrate specificity, yet it displays remarkable resistance to inhibition by blood plasma proteinase inhibitors. In this study we have examined the cleavage of human fibrinogen by tryptase. alpha chain cleavage was shown t...

متن کامل

An antifibrin monoclonal antibody useful in immunoscintigraphic detection of thrombi.

Balb/c mice were immunized with human plasmin-generated fibrinogen degradation product Y. Spleen cells were fused with P3X63-Ag8.653 myeloma cells. A clone (Y22) was found that produces monoclonal antibodies (MoAbs) with a strong reactivity with human fibrin and only a weak reactivity with fibrinogen in an enzyme immunoassay (EIA). Y22 also reacts with fibrin of rabbits, rats, sheep, and dogs. ...

متن کامل

An Ex-Vivo Study on the Stereoselective Accumulation of Mefloquine Enantiomers in Human Blood Fractions

       Mefloquine (MFQ), as a racemic mixture is used for the prophylaxis and treatment of malaria. Stereoselective pharmacodynamic and pharmacokinetic differences have been observed for MFQ. In the present study, the human blood was spiked with racemic MFQ. The concentration of MFQ enantiomers in various blood fractions including packed erythrocyte layer, platelet rich plasma and platelet poor...

متن کامل

Fibrinogen inhibits the heparin cofactor II-mediated antithrombin activity of dermatan sulfate.

Dermatan sulfate is a naturally occurring antithrombotic glycosaminoglycan. The antithrombin activity of several dermatan sulfate preparations has been measured in whole human plasma and found to be -55% of that in purified systems. Kinetic studies under pseudo-first-order conditions indicated that the reduction in antithrombin activity of dermatan sulfate in plasma compared with that in buffer...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The American journal of physiology

دوره 156 3  شماره 

صفحات  -

تاریخ انتشار 1949