Studies of hemophilia; the assay of the antihemophilic clot-promoting principle in normal human plasma with some observations on the relative potency of certain plasma fractions.
نویسندگان
چکیده
Ever since Sahli ( 1 ) demonstrated that the coagulation of hemophilic blood is accelerated by the addition of normal blood 2 many workers (2 to 9) have focused attention on its clot-promoting property. Since cell-free plasma seemed as effective as platelet-rich plasma this action could not be directly attributed to any of the cellular components of blood (2). Hemophilic plasma ws found to be inert. The antihemophilic factors in normal plasma seem to be associated with the globulins and fibrinogen (3 to 7), and appear preponderantly in Fraction I obtained by Cohn and his collaborators (7, 10 to 12). The present communication deals with the quantitative relationship between the amount of normal plasma added to hemophilic blood and the coagulation time of such mixtures. We believe that the observations provide a basis for estimating antihemophilic activity of plasma, and we present them in the hope that they will be extended by others in studies of the coagulation defect of hemophilic blood. Also included are some observations on the potency of certain plasma fractions, which demonstrate the applicability of the relationship to work aimed at the separation of the clot-promoting principle from plasma.
منابع مشابه
Expression of Recombinant Coagulation Factor IX in Human Amniotic Membrane-derived Mesenchymal Stem Cells: A New Strategy to Gene Therapy of Hemophilia B
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متن کاملStudies on the purification of antihemophilic factor (factor VIII). II. Separation of partially purified antihemophilic factor by gel filtration of plasma.
A high degree of purification of antihemophilic factor was achieved by filtration of chylomicronpoor human plasma through columns of agarose. The final product contained, on the average, 67 units of antihemophilic activity per mg of protein, and was 3360-fold purified compared with the filtered plasma. The molecular weight of antihemophilic factor appeared to be at least two million. Preparatio...
متن کاملIi. Separation of Partially Purified Antihemophilic Factor by Gel Filtration of Plasma
product contained, on the average, 67 units of antihemophilic activity per mg of protein, and was 3360-fold purified compared with the filtered plasma. The molecular weight of antihemophilic factor appeared to be at least two million. Preparations separated by gel filtration were contaminated with appreciable amounts of plasma thromboplastin antecedent (PTA), and traces of Christmas factor and ...
متن کاملStudies on the nature of antihemophilic factor (factor VIII). Further evidence relating the AHF-like antigens in normal and hemophilic plasmas.
Normal human antihemophilic factor (AHF, factor VIII) and the protein antigenically related to it in hemophilic plasma both appeared in the void volume of columns of agarose (Sepharose 4B) during purification of these agents. On ultracentrifugation upon sucrose gradients, both agents had sedimentation characteristics similar to those of an S30 marker. After reduction, the polypeptide chains of ...
متن کاملSeparation of Partially Purified Antihemophilic Factor by Gel Filtration of Plasma
product contained, on the average, 67 units of antihemophilic activity per mg of protein, and was 3360-fold purified compared with the filtered plasma. The molecular weight of antihemophilic factor appeared to be at least two million. Preparations separated by gel filtration were contaminated with appreciable amounts of plasma thromboplastin antecedent (PTA), and traces of Christmas factor and ...
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ورودعنوان ژورنال:
- The Journal of clinical investigation
دوره 27 1 شماره
صفحات -
تاریخ انتشار 1948