Modeling the One-Stage Synthesis of Composite Particles of the Nucleus–Shell Type in Separate Oxidation of Titanium and Silicon Tetrachlorides in a Plasmachemical Reactor

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.

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Reference Method for the One-Stage Prothrombin Time Test on Human Blood

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648029 ◽

1976 ◽

Vol 36 (01) ◽

pp. 237-238 ◽

Cited By ~ 44

Author(s):

G. I. C Ingram ◽

M Hills

Keyword(s):

Prothrombin Time ◽

Human Blood ◽

Reference Method ◽

One Stage ◽

Time Test ◽

The One

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The Effects of Amines on the Esterase Activities of Thrombin and Thrombokinase and on Several Clotting Tests

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649165 ◽

1974 ◽

Vol 31 (02) ◽

pp. 309-318

Author(s):

Phyllis S Roberts ◽

Raphael M Ottenbrite ◽

Patricia B Fleming ◽

James Wigand

Keyword(s):

Choline Chloride ◽

Polymerization Process ◽

Ammonium Bromide ◽

Bovine Thrombin ◽

One Stage ◽

Human Proteins ◽

Rate Of Hydrolysis ◽

The One ◽

Hydrolysis Of Esters ◽

Hydrolysis Of

Summary1. Choline chloride, 0.1 M (in 0.25 M Tris. HCl buffer, pH 7.4 or 8.0, 37°), doubles the rate of hydrolysis of TAME by bovine thrombokinase but has no effect on the hydrolysis of this ester by either human or bovine thrombin. Only when 1.0 M or more choline chloride is present is the hydrolysis of BAME by thrombokinase or thrombin weakly inhibited. Evidence is presented that shows that these effects are due to the quaternary amine group.2. Tetramethyl ammonium bromide or chloride has about the same effects on the hydrolysis of esters by these enzymes as does choline chloride but tetra-ethyl, -n.propyl and -n.butyl ammonium bromides (0.1 M) are stronger accelerators of the thrombokinase-TAME reaction and they also accelerate, but to a lesser degree, the thrombin-TAME reaction. In addition, they inhibit the hydrolysis of BAME by both enzymes. Their effects on these reactions, however, do not follow any regular order. The tetraethyl compound is the strongest accelerator of the thrombokinase-TAME reaction but the tetra-ethyl and -butyl compounds are the strongest accelerators of the thrombin-TAME reaction. The ethyl and propyl compounds are the best (although weak) inhibitors of the thrombokinase-BAME and the propyl compound of the thrombin-BAME reactions.3. Tetra-methyl, -ethyl, -n.propyl and -n.butyl ammonium bromides (0.01 M) inhibit the clotting of fibrinogen by thrombin (bovine and human proteins) at pH 7.4, imidazole or pH 6.1, phosphate buffers and they also inhibit, but to a lesser degree, a modified one-stage prothrombin test. In all cases the inhibition increases regularly as the size of the alkyl group increases from methyl to butyl. Only the ethyl com pound (0.025 M but not 0.01 M), however, significantly inhibits the polymerization of bovine fibrin monomers. It was concluded that inhibition of the fibrinogen-thrombin and the one-stage tests by the quaternary amines is not due to any effect of the com pounds on the polymerization process but probably due to inhibition of thrombin’s action on fibrinogen by the quaternary amines.

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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

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654555 ◽

1961 ◽

Vol 6 (02) ◽

pp. 224-234 ◽

Cited By ~ 4

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.

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The Preparation of an Artificial Reagent for the One-Stage Factor VIII Assay

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654144 ◽

1970 ◽

Vol 23 (02) ◽

pp. 306-312 ◽

Cited By ~ 7

Author(s):

D Nyman

Keyword(s):

Factor Viii ◽

Artificial Substrate ◽

One Stage ◽

The One

SummaryA method for preparation of an artificial substrate for the one-stage factor VIII assay is described. Standardization of the test is given. The method is specific and reproducible.

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The Reaction of Thiol Compounds with the Vitamin-K Dependent Clotting Factors

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653570 ◽

1969 ◽

Vol 21 (03) ◽

pp. 573-579 ◽

Cited By ~ 1

Author(s):

P Fantl

Keyword(s):

Prothrombin Time ◽

Vitamin K ◽

Anaerobic Conditions ◽

Clotting Factors ◽

Thiol Compounds ◽

Aerobic Conditions ◽

One Stage ◽

Factor Ii ◽

Ph Dependent ◽

The One

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.

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Two-Stage Procedure for the Quantitative Determination of Autoprothrombin III Concentration and Some Applications

Thrombosis and Haemostasis ◽

10.1055/s-0038-1655029 ◽

1967 ◽

Vol 18 (01/02) ◽

pp. 198-210 ◽

Cited By ~ 5

Author(s):

Ronald S Reno ◽

Walter H Seegers

Keyword(s):

Prothrombin Time ◽

Factor Vii ◽

Two Stage ◽

Pronounced Increase ◽

One Stage ◽

Assay Procedure ◽

Bovine Plasma ◽

The One ◽

Autoprothrombin C

SummaryA two-stage assay procedure was developed for the determination of the autoprothrombin C titre which can be developed from prothrombin or autoprothrombin III containing solutions. The proenzyme is activated by Russell’s viper venom and the autoprothrombin C activity that appears is measured by its ability to shorten the partial thromboplastin time of bovine plasma.Using the assay, the autoprothrombin C titre was determined in the plasma of several species, as well as the percentage of it remaining in the serum from blood clotted in glass test tubes. Much autoprothrombin III remains in human serum. With sufficient thromboplastin it was completely utilized. Plasma from selected patients with coagulation disorders was assayed and only Stuart plasma was abnormal. In so-called factor VII, IX, and P.T.A. deficiency the autoprothrombin C titre and thrombin titre that could be developed was normal. In one case (prethrombin irregularity) practically no thrombin titre developed but the amount of autoprothrombin C which generated was in the normal range.Dogs were treated with Dicumarol and the autoprothrombin C titre that could be developed from their plasmas decreased until only traces could be detected. This coincided with a lowering of the thrombin titre that could be developed and a prolongation of the one-stage prothrombin time. While the Dicumarol was acting, the dogs were given an infusion of purified bovine prothrombin and the levels of autoprothrombin C, thrombin and one-stage prothrombin time were followed for several hours. The tests became normal immediately after the infusion and then went back to preinfusion levels over a period of 24 hrs.In other dogs the effect of Dicumarol was reversed by giving vitamin K1 intravenously. The effect of the vitamin was noticed as early as 20 min after administration.In response to vitamin K the most pronounced increase was with that portion of the prothrombin molecule which yields thrombin. The proportion of that protein with respect to the precursor of autoprothrombin C increased during the first hour and then started to go down and after 3 hrs was equal to the proportion normally found in plasma.

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