Merck Patent Gesellschaft MIT Beschrankter Haftung

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Norbert Hennrich

Hermann Lang

Hans-Dieter Orth

Uwe Wurzburg

Wolfgang Brummer

Gerhard Pfleiderer

Hans Dieter Orth

Michael Klockow

Roland Helger

Siegfried Neumann

Wolfgang Ebeling

Kurt Ingemar Lundstrom

Gunter Sielaff

Dieter Banauch

Hans Pauly

Evangelista Jockers-Wretou

Hans R Arwin

Erwin Rieke

A process, means and devices for the quantitative determination, using electromagnetic radiation, of a component of a group including specifically bonding receptors and substances which can be specifically bonded by these receptors are based on a process comprising incubating one of the components, after it is immobilizing on the surface of a material having refractive index different from that of the components, with the other particular component and, optionally, further components, which can be labelled; irradiating the surface with electromagnetic radiation which is polarized parallel to the plane of incidence, the angle of incidence of the radiation being approximately equal to the angle .PHI. at which the intensity of the radiation reflected from the uncoated or precoated surface reaches a minimum; and ascertaining the intensity of the reflected radiation as a measure of the concentration to be determined.

Optical specific binding assay with reflection of polarized

A process for the quantitative immunological determination of an enzyme in a liquid, comprises incubating anti-enzyme antibodies which are adsorbed on a water-insoluble carrier, with the sample solution containing the enzyme, whereby the enzyme bonds to the antibodies but retains a reproducible proportion of its activity in its complex with the antibodies; removing the sample solution; washing the antibody carrier, which is charged with enzyme; and determining the activity of the enzyme bonded to the antibodies.

Method and agent for the immunological determination of enzymes

Antibodies against the M subunit of CK isoenzymes having a molecular weight between about 130,000 and 210,000, and inhibiting the enzymatic activity of the M subunit, optionally also in the presence of CK substrates, without inactivating the enzymatic activity of the B subunit of any CK-MB which may be present, are described. A process for the production of these antibodies comprises inoculating animals with activated CK-MM and recovering the antibodies in a conventional manner.

Antibodies against creatinekinase-M8 and process for the production

A process for determination of CK-MB activity in a sample of a body fluid comprising the steps of incubating the sample, optionally in the presence of CK substrates, with antibodies which inhibit enzymatic activity of the M subunit in CK isoenzymes MM and MB without inactivating enzymatic activity of the B subunit in any CK-MB which may be present and determining the activity of the CK B subunit in the resultant sample.

Process and composition for determining the activity of creatinekinase-MB

Isoenzyme patterns of an enzyme in biological fluids, extracts, and/or excretions are quantitatively determined by precipitating at least 90% of an isoenzyme antigen with a corresponding heterologous antiserum and comparing the remaining enzyme activity with the total activity with the use of a conventional agent for enzyme activity determination.

Analysis of isoenzyme patterns

Glucose is rapidly ad quantitatively determined with an analytical agent containing glucose dehydrogenase having an activity of at least 2 .mu./mg and NADH.sub.2 oxidase activity less than 0.1%, a pyridine coenzyme, a buffer and mutarotase to increase spontaneous mutarotation of alpha-glucose to beta-glucose. There may be optionally present inhibitors for reduced pyridine coenzyme oxidases and a thermal stabilizing amount of alkali metal chloride.

Enzymatic determination of glucose

Biochemically active compounds e.g., proteins and particulate biological materials such as bacteria and viruses, are immobilized on a water-swellable or water-insoluble matrix by covalent bonding to a partially crosslinked polymer containing reactive groups capable of binding the biochemically active compound thereto.

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Darmstadt, Germany

Norbert Hennrich