Abstract:
Spontaneous aspecific coloration in so-called Trinder reagents which can alter subsequent colorimetric determinations is inhibited by adding compounds of the chelating agent class to the solution. The resultant compositions contain a peroxidase enzyme, a phenylpyrazone derivative, a compound of phenolic or aromatic amine structure and a stabilizer. Preferred stabilizers are ethylenediaminetetraacetic acid (EDTA) and diethylenetriaminepentaacetic acid (DTPA).
Abstract:
The present invention provides a method for determining thrombotic risk in an individual. The method involves determining the activity of Protein C and Protein S in the plasma of the individual thought to be at thrombotic risk by adding to a plasma sample obtained from the individual: (i) a first reagent in an amount sufficient to induce or activate coagulation in the plasma, (ii) a second reagent which activates endogenous protein C in the plasma, and (iii) a third reagent comprising calcium salts, phospholipids or tissue thromboplastin, or a combination thereof. To a second plasma sample from the same subject is added a reagent which induces or activates coagulation, and a buffer or other material which does not activate protein C, and a third reagent as described above. The time, rate or both, necessary for the conversion of endogenous fibrinogen to fibrin in both the first and second samples is measured. The same steps are performed on normal control plasma, and the difference or ratio in the times, rates, or both, obtained above are determined. The difference or ratio is indicative of the thrombotic risk in the subject. A kit adapted to carry out the method also is the subject of the present invention. The methods and kits of the invention in other embodiments may comprise a first reagent comprising a synthetic substrate, a second reagent which in the first sample from the subject activates protein C, and in the second sample, a second reagent which does not activate protein C. In these embodiments, the rates of hydrolysis of the synthetic substrates are measured and compared.
Abstract:
Liquid and lyophilized reagents for determining prothrombin time and/or fibrinogen levels in a plasma sample are disclosed. The reagents preferably are based on recombinant rabbit tissue factor. Also disclosed is a purified preparation of recombinant rabbit tissue factor having unique properties, and a novel method for making PT reagents.
Abstract:
The present invention provides a method for determining thrombotic risk in an individual. The method involves determining the activity of Protein C and Protein S in the plasma of the individual thought to be at thrombotic risk by adding to a plasma sample obtained from the individual (i) a first reagent in an amount sufficient to induce or activate coagulation in the plasma, (ii) a second reagent which activates endogenous protein C in the plasma, and (iii) a third reagent comprising calcium salts, phospholipids or tissue thromboplastin, or a combination thereof. To a second plasma sample from the same subject is added a reagent which induces or activates coagulation, and a buffer or other material which does not activate protein C, and a third reagent as described above. The time, rate or both, necessary for the conversion of endogenous fibrinogen to fibrin in both the first and second samples is measured. The same steps are performed on normal control plasma, and the difference or ratio in the times, rates, or both, obtained above are determined. The difference or ratio is indicative of the thrombotic risk in the subject. A kit adapted to carry out the method also is the subject of the present invention. The methods and kits of the invention in other embodiments may comprise a first reagent comprising a synthetic substrate, a second reagent which in the first sample from the subject activates protein C, and in the second sample, a second reagent which does not activate protein C. In these embodiments, the rates of hydrolysis of the synthetic substrates are measured and compared.
Abstract:
An aqueous coenzyme reagent composition contains NADH, a carbonate/bicarbonate buffer (with a pH of about 9.5-11) and water. Both NADH and the buffer are at low concentrations, e.g., about 2-5 mM for NADH and about 2-15 mM for carbonate/bicarbonate. When this coenzyme reagent is mixed with an enzyme reagent, the mixture achieves a neutral pH. The combination of high pH, low NADH concentration and low buffer concentration permit the aqueous reagent to be stored for extended periods at low temperatures without NADH degrading to form impurities which interfere with or inhibit enzyme activity, such as the activity of lactate dehydrogenase or malate dehydrogenase in an assay for ALT or AST.
Abstract:
In a single-use device for collecting and holding blood samples, provision is made for an evacuated tube with a closure (stopper) that can be pierced by the tip of a needle, the other tip of which is intended to be inserted into a vein of a patient. Disposed below the said pierceable stopper, and in the tube, is a diaphragm intended to passed through by the needle-tip that pierces the stopper, so as to form a supplementar barrier between the interior of the tube and the environment when the pierceable stopper is removed.