Performances of an Artificial Reagent for the One-stage Factor IX Assay

1975 ◽  
Vol 33 (03) ◽  
pp. 547-552 ◽  
Author(s):  
L Meunier ◽  
J. P Allain ◽  
D Frommel
Keyword(s):  
Human Plasma ◽  
Factor Ix ◽  
Severe Haemophilia ◽  
Normal Human Plasma ◽  
Haemophilia B ◽  
One Stage ◽  
Normal Human ◽  
The One

SummaryA mixture of adsorbed normal human plasma and chicken plasma was prepared as reagent for factor IX measurement using a one-stage method. The substrate was found to be specific for factor IX. Its performances tested on samples displaying factor IX activity ranging from <l%–2,500% compared favorably with those obtained when using the plasma of severe haemophilia B patients as substrate.

Immunological Method for the Detection of the Carrier of Haemophilia B.

1975 ◽  
Author(s):  
M. Matsuoka ◽  
M. Ito ◽  
N. Sakuragawa ◽  
K. Takahashi
Keyword(s):  
North Carolina ◽  
Factor Ix ◽  
Haemophilia A ◽  
Severe Haemophilia ◽  
Normal Human Plasma ◽  
Sephadex Column ◽  
Haemophilia B ◽  
The North ◽  
Normal Human ◽  
Almost All

Both the immunoassay and bioassay were performed on factor IX activity of haemophilia B patient. Their values were compared with each other.The immunoassay by neutralization was performed as follows: antibody to factor IX was obtained by immunization of purified factor IX to rabbit which was isolated by the technique of DEAE-Sephadex column chromatography using eluate from BaS04 which absorbed factor IX of normal human plasma.In approximately 90% of the cases of definite carriers of haemophilia B, the activity of factor IX by bioassay was observed to be lower than that of factor VIII of haemophilia A carrier. The factor IX activity was observed to be at the same level as factor IX antigen by immunoassay in almost all of the cases, but in the cases of the mother of haemophilia B, and the North Carolina type of haemophilia B the factor IX antigen was much greater than that of activity by bioassay. The same results were obtained by the above mentioned methods using inhibitor substance arising from severe haemophilia B patient.It was suggested that the immunoassay method is useful in detecting the carrier of haemophilia B and North Carolina type of haemophilia B.

The Formation of Intermediate Product I in a Purified System The Role of Factor IX or of its Precursor and of a Hageman Factor-PTA Fraction

1961 ◽  
Vol 6 (02) ◽  
pp. 224-234 ◽  
Author(s):  
E. T Yin ◽  
F Duckert
Keyword(s):  
Intermediate Product ◽  
Factor Ix ◽  
Assay Method ◽  
Lag Phase ◽  
Factor X ◽  
Haemophilia B ◽  
Hageman Factor ◽  
One Stage ◽  
The One

Summary1. The role of two clot promoting fractions isolated from either plasma or serum is studied in a purified system for the generation of intermediate product I in which the serum is replaced by factor X and the investigated fractions.2. Optimal generation of intermediate product I is possible in the purified system utilizing fractions devoid of factor IX one-stage activity. Prothrombin and thrombin are not necessary in this system.3. The fraction containing factor IX or its precursor, no measurable activity by the one-stage assay method, controls the yield of intermediate product I. No similar fraction can be isolated from haemophilia B plasma or serum.4. The Hageman factor — PTA fraction shortens the lag phase of intermediate product I formation and has no influence on the yield. This fraction can also be prepared from haemophilia B plasma or serum.

Pharmacokinetics of a new human plasma‐derived double virus inactivated and nanofiltered factor IX concentrate in previously treated severe or moderately severe haemophilia B patients

Haemophilia ◽  
2019 ◽  
Vol 25 (6) ◽  
Author(s):  
Giancarlo Castaman ◽  
Alessandra Borchiellini ◽  
Elena Santagostino ◽  
Giuseppe Tagariello ◽  
Margit Serban ◽  
...  
Keyword(s):  
Human Plasma ◽  
Factor Ix ◽  
Severe Haemophilia ◽  
Haemophilia B ◽  
Previously Treated

scholarly journals Artificial Substrate Plasma for the Specific One-Stage Factor X Assay

1977 ◽  
Author(s):  
H. Beeser ◽  
R. Kulzer
Keyword(s):  
Artificial Substrate ◽  
Factor X ◽  
Normal Human Plasma ◽  
One Stage ◽  
Factor X Deficiency ◽  
Factor Ii ◽  
Normal Human ◽  
Plasma Methods ◽  
The One ◽  
Congenital Factor

As patients who are congenitally deficient in factor X are extremely rare natural substrate plasma for the specific one-stage factor X assay is only poorly available. Asbestos-filtered or charcoal-filtered ox plasma deficient both in factor X and VII is instead widely used as artificial factor X substrate plasma with Russel’s viper venom (BW) and cephalin or lecithin as the thromboplastic agent.We studied the practicability of removing separately factor X from the plasma of different species (man, horse, ox, sheep, swine) by several chromatographic procedures. Chromatography of swine plasma on DEAE-Sephadex A 25 yielded a substrate virtually free of factor X while containing adequate concentrations of fibrinogen and factor II, V and VII, Using different brands of commercial tissue thromboplastins the so prepared swine plasma has proved to be a specific artificial substrate plasma for the one-stage factor X assay. Calibration curves obtained by plotting the clotting times of various dilutions of pooled normal human plasma determined with this factor X assay system against the percentages showed a linear relationship from 100% to about 2% on log/log paper. Factor X determinations with our method on various patients’ plasmas (i.e. coumarin treatment, congenital factor X deficiency, liver disease) performed in parallel to the RVV-cephalin and the congenital factor X deficient plasma methods gave comparable results.As our specific artificial factor X deficient swine plasma is fairly simple prepared with a good yield, it has to be considered as an appropriate reagent to overcome the shortness of the rare congenital factor X deficient substrate plasma.

The Prephase Accelerator. Present Status

1961 ◽  
Vol 6 (02) ◽  
pp. 254-260 ◽  
Author(s):  
F Duckert
Keyword(s):  
Present Status ◽  
Factor Ix ◽  
Quantitative Assay ◽  
Assay Method ◽  
Clotting Factors ◽  
Haemophilia B ◽  
Hageman Factor ◽  
One Stage ◽  
The One ◽  
Generation Test

SummaryThe properties of the prephase accelerator (PPA) are indicated as well as its differentiation from other known clotting factors. PPA is either a reaction product or a degratation product. For its normal formation genuine factor IX, PTA and ? Hageman factor are necessary.The one-stage quantitative assay method for factor “IX” does not determine the factor lacking in haemophilia B. This method gives a measure of PPA.Some practical observations are made concerning the value of the one-stage assay method for factor “IX” and of the thromboplastin generation test for the diagnosis of haemophilia B.

Plasma Components which Interfere with Ristocetin-induced Platelet Aggregation

1975 ◽  
Vol 33 (03) ◽  
pp. 540-546 ◽  
Author(s):  
Robert F Baugh ◽  
James E Brown ◽  
Cecil Hougie
Keyword(s):  
Platelet Aggregation ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Binding Protein ◽  
Plasma Heating ◽  
Protein S ◽  
Fold Increase ◽  
Normal Human Plasma ◽  
Preliminary Examination ◽  
Normal Human

SummaryNormal human plasma contains a component or components which interfere with ristocetin-induced platelet aggregation. Preliminary examination suggests a protein (or proteins) which binds ristocetin and competes more effectively for ristocetin than do the proteins involved in ristocetin-induced platelet aggregation. The presence of this protein in normal human plasma also prevents ristocetin-induced precipitation of plasma proteins at levels of ristocetin necessary to produce platelet aggregation (0.5–2.0 mg/ml). Serum contains an apparent two-fold increase of this component when compared with plasma. Heating serum at 56° for one hour results in an additional 2 to 4 fold increase. The presence of a ristocetin-binding protein in normal human plasma requires that this protein be saturated with ristocetin before ristocetin-induced platelet aggregation will occur. Variations in the ristocetin-binding protein(s) will cause apparent discrepancies in ristocetin-induced platelet aggregation in normal human plasmas.

Analysis of Intrinsic Fibrinolysis in Human Plasma Induced by Dextran Sulfate

1992 ◽  
Vol 67 (04) ◽  
pp. 440-444 ◽  
Author(s):  
Hiroko Tsuda ◽  
Toshiyuki Miyata ◽  
Sadaaki Iwanaga ◽  
Tetsuro Yamamoto
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
Dextran Sulfate ◽  
Tissue Type ◽  
Factor Xii ◽  
Normal Human Plasma ◽  
High Molecular Weight Kininogen ◽  
Single Chain ◽  
Major Pathway ◽  
Normal Human

SummaryThe analysis of normal human plasma by fibrin autography revealed four species of plasminogen activator (PA) activity related to tissue-type PA, factor XII, prekallikrein and urokinase-type PA (u-PA). The u-PA activity increased significantly by incubating plasma with dextran sulfate. This increase was coincident with both the cleavage of factor XII and the complex formation of activated factor XII with its plasma inhibitors, which were determined by immunoblotting procedure. The dextran sulfate-dependent activation of u-PA required both factor XII and prekallikrein, but did not require either plasminogen or factor XI. High molecular weight kininogen was required only at a low concentration of dextran sulfate. Thus the results indicate that the factor XII and prekallikrein-mediated activation of single chain u-PA (scu-PA) operates as a major pathway of scu-PA activation in whole plasma in contact with dextran sulfate.

Presence and Possible Origin of ɛ(γ-Glutamyl)Lysine Isodipeptide in Human Plasma

1992 ◽  
Vol 67 (01) ◽  
pp. 060-062 ◽  
Author(s):  
J Harsfalvi ◽  
E Tarcsa ◽  
M Udvardy ◽  
G Zajka ◽  
T Szarvas ◽  
...  
Keyword(s):  
Human Plasma ◽  
Fibrinolytic Therapy ◽  
Normal Human Plasma ◽  
Normal Human ◽  
Hplc Technique ◽  
Significant Change

Summaryɛ(γ-glutamyl)lysine isodipeptide has been detected in normal human plasma by a sensitive HPLC technique in a concentration of 1.9-3.6 μmol/1. Incubation of in vitro clotted plasma at 37° C for 12 h resulted in an increased amount of isodipeptide, and there was no further significant change when streptokinase was also present. Increased in vivo isodipeptide concentrations were also observed in hypercoagulable states and during fibrinolytic therapy.

Management of Haemophilia in Sweden

1976 ◽  
Vol 35 (03) ◽  
pp. 510-521 ◽  
Author(s):  
Inga Marie Nilsson
Keyword(s):  
Factor Viii ◽  
Total Population ◽  
Age Groups ◽  
Factor Ix ◽  
Haemophilia A ◽  
Severe Haemophilia ◽  
Haemophilia B ◽  
Human Fraction ◽  
Mild Haemophilia

SummaryThe incidence of living haemophiliacs in Sweden (total population 8.1 millions) is about 1:15,000 males and about 1:30,000 of the entire population. The number of haemophiliacs born in Sweden in 5-year periods between 1931-1975 (June) has remained almost unchanged. The total number of haemophilia families in Sweden is 284 (77% haemophilia A, 23% haemophilia B) with altogether 557 (436 with A and 121 with B) living haemophiliacs. Of the haemophilia A patients 40 % have severe, 18 % moderate, and 42 % mild, haemophilia. The distribution of the haemophilia B patients is about the same. Inhibitors have been demonstrated in 8% of the patients with severe haemophilia A and in 10% of those with severe haemophilia B.There are 2 main Haemophilia Centres (Stockholm, Malmo) to which haemophiliacs from the whole of Sweden are admitted for diagnosis, follow-up and treatment for severe bleedings, joint defects and surgery. Minor bleedings are treated at local hospitals in cooperation with the Haemophilia Centres. The concentrates available for treatment in haemophilia A are human fraction 1-0 (AHF-Kabi), cryoprecipitate, Antihaemophilic Factor (Hyland 4) and Kryobulin (Immuno, Wien). AHF-Kabi is the most commonly used preparation. The concentrates available for treatment in haemophilia B are Preconativ (Kabi) and Prothromplex (Immuno). Sufficient amounts of concentrates are available. In Sweden 3.2 million units of factor VIII and 1.0 million units of factor IX are given per year. Treatment is free of charge.Only 5 patients receive domiciliary treatment, but since 1958 we in Sweden have practised prophylactic treatment of boys (4–18 years old) with severe haemophilia A. At about 5-10 days interval they receive AHF in amounts sufficient to raise the AHF level to 40–50%. This regimen has reduced severe haemophilia to moderate. The joint score is identical with that found in moderate haemophilia in the same age groups. For treatment of patients with haemophilia A and haemophilia B complicated by inhibitors we have used a large dose of antigen (factor VIII or factor IX) combined with cyclophosphamide. In most cases this treatment produced satisfactory haemostasis for 5 to 30 days and prevented the secondary antibody rise.

Investigations on the Nature of Hemophilia A

1963 ◽  
Vol 09 (01) ◽  
pp. 030-052 ◽  
Author(s):  
Eberhard Mammen
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Barium Sulfate ◽  
Freeze Drying ◽  
Room Temperature ◽  
Hemophilia A ◽  
Normal Human Plasma ◽  
Normal Human ◽  
And Storage ◽  
Prothrombin Activation

SummaryIn this paper an inhibitor is described that is found in hemophilic plasma and serum different from any till now described inhibitor. The inhibitor only inhibits prothrombin activation in the “intrinsic clotting systems”. This inhibitor is probably not present in normal human plasma or serum. It is destroyed by ether and freeze drying, is labile to acid and storage at room temperature. It is stable upon dialysis and has not been adsorbed on barium sulfate, aluminum hydroxide or kaolin. It precipitates at 50% v/v saturation with alcohol. The nature of this inhibitor seems to be a protein or lipoprotein.Factor VIII was isolated from hemophilic plasma. The amount isolated was the same as from normal plasma and the activity properties were not different. Hemophiliacs have normal amounts of factor VIII.

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