Boehringer Mannheim Gmbh

Peter Roeschlau

Wolfgang Gruber

Gunter Lang

Erich Bernt

Klaus Beaucamp

Udo Becker

Joachim Ziegenhorn

Ulfert Deneke

Hans Seidel

Knut Bartl

Helmut Lill

Alexander Hagen

Michael Nelboeck-Hochstetter

Helmut Jering

Hans Ulrich Bergmeyer

Gerhard Michal

Helmut Rehner

Detlef Von Hoerschelmann

Dieter Hundt

Michael Klarwein

Josef Danninger

Control serum containing (1) at least one compound of the formula: ##STR1## in which T is hydrogen or methyl, hydroxymethyl or methoxymethyl

Control serum and process therefor

The present invention provides a process for the simultaneous determination of fibrinogen and fibrinogen fission products in plasma, wherein 0.01 to 1 U of a snake venom enzyme with a thrombin-like effectiveness is aded per ml. of sample plasma, then there is measured the period of time between the addition of the enzyme and the commencement of a turbidity formation as a measure for the amount of fibrinogen fission products and subsequently there is measured the speed of the turbidity formation as a measure of the amount of fibrinogen. The present invention also provides a reagent for the simultaneous determination of fibrinogen and fibrinogen fission products, wherein it comprises 0.01 to 10 U snake venon enzyme with thrombin-like effectiveness per ml. of sample plasma, 0.5 to 4% by weight of a water-soluble polyalcohol, 1 to 20 mMole/liter of calcium ions and 0.05 to 0.3 mole/liter of buffer of pH 7.0 to 8.0, referred to the solution ready for use, as well as optionally a detergent.

Process and a reagent for the simultaneous determination of fibrinogen

The present invention provides a reagent for the optical determination of blood coagulation behavior (Quick test), comprising thromboplastin, a synthetic thrombin substrate and a buffer, characterized by a content of non-proteolytically active thromboplastin.

Reagent for the optical determination of the blood coagulation

The present invention provides a process for the detection or determination of fibrin monomer in biological fluids, wherein the sample fluid is incubated with hydrophobic latex and the agglutination determined. The present invention also provides a reagent for the detection or determination of fibrin or fibrin monomer in biological fluids, wherein it contains hydrophobic latex.

Method and reagent for the detection of fibrin monomer

Method and reagent for the determination of the biological activity of heparin in plasma by adding thrombin or Factor X.sub.a as the proteolytic enzyme and a chromogen substrate of the latter and measuring the dye liberated from the chromogen substrate in the absence of exogenous anti-thrombin III, the improvement consisting of adding, additionally, at least one compound of the formula ##STR1## wherein X is oxygen or the group NR.sub.5 ;

Process and reagent for the determination of the biological activity of

Cholesterol is determined by incubating a sample suspected of containing cholesterol in an aqueous medium with cholesterol oxidase and determining either the oxygen consumption, the hydrogen peroxide formed, or cholestenone, as a measure of the initial cholesterol content; reagent compositions comprising cholesterol oxidase and a system for the determination of H.sub.2 O.sub.2 or for the determination of cholestenone are provided.

Reagent and method for the determination of cholesterol

Cholesterol is determined utilizing cholesterol oxidase, and optionally cholesterol esterase to cleave bound cholesterol, in the presence of peroxidase, p-amino-phenazone, a surface-active agent and phenol, the improvement comprising employing an alkanol of up to 4 carbon atoms in the test composition or sample to substantially overcome test error and deviations due to turbidity formation.

Process and reagent for determining cholesterol

In a process for the determination of total or bound cholesterol by liberating any bound cholesterol using cholesterol esterase and simultaneously or subsequently determining the liberated cholesterol and any initially free cholesterol with a cholesterol reacting enzyme, the improvement comprising using as the cholesterol reacting enzyme an NAD or NADP-dependent cholesterol dehydrogenase obtained from an anaerobic microorganism, e.g., Eubacterium sp. ATCC 21408, or from mammalian tissue, e.g., liver.

Composition and method for the determination of cholesterol

In a process for the determination of substrates or enzyme activities in a test batch, utilizing a conventional redox reaction as a measurement reaction, the improvement comprising carrying out the process in the presence of ascorbate oxidase; the addition of ascorbate oxidase substantially eliminates the interfering effect of ascorbic acid frequently found in the test sample.

Method for the determination of substrates or enzyme activities

Cholesterol oxidase free of unstabilizing residual traces of detergent is activated by adding to the cholesterol oxidase, before use thereof, at least one surface-active compound with lipophilic and hydrophilic properties. Diagnostic agents for determining cholesterol comprising cholesterol oxidase, a hydrogen peroxide detection system, a buffer, and at least one surface-active compound having lipophilic and hydrophilic properties are provided.

Activation of cholesterol oxidase for cholesterol assay

The activity of alkaline phosphatase in aqueous solution, especially in reconstituted serum, is kept constant by adding to the phosphatase-containing solution Mn.sup.2+ or Cd.sup.2+ ions, preferably to an end concentration of 0.05 to 0.5 mMol/liter of Mn.sup.2+ or 0.05 to 0.1 mMol/liter of Cd.sup.2+. Control serums comprising the Mn.sup.2+ and/or Cd.sup.2+ ions in human or animal serum or serum-like compositions are also provided.

Control serum containing alkaline phosphatase of constant activity

The new enzyme steroid-.DELTA.-isomerase is provided, as well as a process for producing same, comprising digesting a micro-organism containing said isomerase, extracting same by destruction of the cell wall with a buffer solution containing a non-ionic surfactant, centrifuging the resulting mass and discarding the precipitate, applying the extract to an anion exchanger, eluting the enzyme with a buffer solution containing a non-ionic surfactant, heating the eluate, separating the precipitate and isolating the enzyme therefrom from the supernatant.

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Seeshaupt, Germany

Peter Roeschlau