Treatment of Hemophilia A with Plasma Fraction I

2015 ◽  
pp. 1301-1302
Author(s):  
E. Gugler
Keyword(s):  
Hemophilia A ◽  
Plasma Fraction ◽  
Fraction I

scholarly journals Properdin: Preparation from Plasma Fraction I of the Cohn Method

1959 ◽  
Vol 234 (4) ◽  
pp. 838-840
Author(s):  
Daniel S. Spicer ◽  
Lois I. Priester ◽  
Edward V.C. Smith ◽  
Benjamin E. Sanders
Keyword(s):  
Plasma Fraction ◽  
Fraction I

scholarly journals Evaluation of the role of in vivo proteolysis (fibrinogenolysis) in prolonging the thrombin time of human umbilical cord fibrinogen

Blood ◽  
1976 ◽  
Vol 48 (1) ◽  
pp. 109-118 ◽  
Author(s):  
DK Galanakis ◽  
MW Mosesson
Keyword(s):  
Ionic Strength ◽  
Umbilical Cord ◽  
Terminal Region ◽  
Human Umbilical Cord ◽  
Thrombin Time ◽  
Alpha Chain ◽  
Plasma Fraction ◽  
Adult Plasma ◽  
Fraction I

Abstract These studies have been directed at evaluating the role played by proteolysis (fibrinogenolysis) in vivo in prolonging the thrombin time of human umbilical cord (“fetal”) fibrinogen. The aggregation rate of cord fibrin compared with that from adult plasma is always delayed when the reaction is carried out under conditions of relatively high ionic strength (e.g., 0.29); this difference is not apparent at relatively low ionic strength (e.g., 0.09). In addition, as assessed by turbidimetric techniques, the maximum absorbance attained by cord fibrin is considerably less than that attained by adult fibrin. Coagulable fibrinogen catabolites (i.e., fraction I-5) are present in cord plasma and, like their counterparts from adult plasma, lack various portions of the COOH-terminal region of the A alpha chain. However, their presence in plasma does not explain the behavioral differences between cord and adult fibrin. Moreover, differences revealed by turbidimetric comparison of cord and adult fibrin from plasma fraction I-2 persist in fibrin from fraction I-5; it therefore appears that the COOH-terminal region of the A alpha chain does not contain the structure(s) accounting for the unique behavior of “fetal” fibrinogen.

scholarly journals Immunologic Studies of Antihemophilic Factor (AHF, Factor VIII) II. Properties of Cross-reacting Material

Blood ◽  
1970 ◽  
Vol 35 (6) ◽  
pp. 809-820 ◽  
Author(s):  
LEON W. HOYER ◽  
ROBERT T. BRECKENRIDGE
Keyword(s):  
Calcium Phosphate ◽  
Physical Properties ◽  
Factor Viii ◽  
Barium Sulfate ◽  
Genetic Variant ◽  
Hemophilia A ◽  
Procoagulant Activity ◽  
Normal Plasma ◽  
Fraction I ◽  
Antihemophilic Factor

Abstract Patients with a genetic variant of hemophilia A have in their plasmas material which has antigenic characteristics similar to those of antihemophilic factor (AHF). The physical properties of the biologically inactive cross-reacting material (CRM) are like those of AHF from normal plasma. The CRM is concentrated in Cohn fraction I and in cryoprecipitates and is not adsorbed from plasma by calcium phosphate or barium sulfate. It is inactivated by heating to 56° for 30 minutes. The CRM is less sensitive to thrombin inactivation than AHF and is recovered in serum. The similar properties of AHF and CRM support the hypothesis that patients with this genetic variant of hemophilia A synthesize a material similar to AHF but lacking procoagulant activity.

The Non-clotting Component of the Human Plasma Fraction I-1 (“Cold Insoluble Globulin”)1

1955 ◽  
Vol 77 (1) ◽  
pp. 157-161 ◽  
Author(s):  
John T. Edsall ◽  
Geoffrey A. Gilbert ◽  
Harold A. Scheraga
Keyword(s):  
Human Plasma ◽  
Plasma Fraction ◽  
Cold Insoluble Globulin ◽  
Fraction I

High Frequency of Low Plasma Haptoglobin Values Found in Hemophilia A Patients on Prophylactic Treatment with Factor VIII Concentrates - A Sign of Hemolysis?

1981 ◽  
Vol 46 (02) ◽  
pp. 554-557 ◽  
Author(s):  
Nils Egberg ◽  
Margareta Blombäck
Keyword(s):  
Factor Viii ◽  
High Purity ◽  
High Frequency ◽  
Prophylactic Treatment ◽  
Hemophilia A ◽  
Factor Viii Concentrates ◽  
Fraction I ◽  
Elevated Lactate ◽  
Elevated Lactate Dehydrogenase ◽  
Plasma Haptoglobin

SummaryLow plasma haptoglobin values have been observed in hemophilia A patients on regular prophylactic treatment with factor VIII concentrates. Two of 3 patients treated with fraction I-0 (Kabi) and 7 of 11 patients treated with high-purity concentrates (Hyland) had low haptoglobin values. Four of 8 patients who were treated with high-purity concentrates prescreened for a low content of anti-A and anti-B immunoglobulins still showed low haptoglobin levels. Unexpectedly, 2 patients of blood group 0 showed low haptoglobin values. The presence of irregular erythrocyte alloantibodies and/or other contaminants of the concentrates might thus also be a cause of hemolysis resulting in an increased consumption of haptoglobin.Elevated lactate dehydrogenase levels were also frequent. No correlations were found between albumin, aspartate or alanine aminotransferase levels and haptoglobin levels.

scholarly journals Evaluation of the role of in vivo proteolysis (fibrinogenolysis) in prolonging the thrombin time of human umbilical cord fibrinogen

Blood ◽  
1976 ◽  
Vol 48 (1) ◽  
pp. 109-118
Author(s):  
DK Galanakis ◽  
MW Mosesson
Keyword(s):  
Ionic Strength ◽  
Umbilical Cord ◽  
Terminal Region ◽  
Human Umbilical Cord ◽  
Thrombin Time ◽  
Alpha Chain ◽  
Plasma Fraction ◽  
Adult Plasma ◽  
Fraction I

These studies have been directed at evaluating the role played by proteolysis (fibrinogenolysis) in vivo in prolonging the thrombin time of human umbilical cord (“fetal”) fibrinogen. The aggregation rate of cord fibrin compared with that from adult plasma is always delayed when the reaction is carried out under conditions of relatively high ionic strength (e.g., 0.29); this difference is not apparent at relatively low ionic strength (e.g., 0.09). In addition, as assessed by turbidimetric techniques, the maximum absorbance attained by cord fibrin is considerably less than that attained by adult fibrin. Coagulable fibrinogen catabolites (i.e., fraction I-5) are present in cord plasma and, like their counterparts from adult plasma, lack various portions of the COOH-terminal region of the A alpha chain. However, their presence in plasma does not explain the behavioral differences between cord and adult fibrin. Moreover, differences revealed by turbidimetric comparison of cord and adult fibrin from plasma fraction I-2 persist in fibrin from fraction I-5; it therefore appears that the COOH-terminal region of the A alpha chain does not contain the structure(s) accounting for the unique behavior of “fetal” fibrinogen.

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