Translation of "Glutamate dehydrogenase" in German

The turbidity stability of glutamate dehydrogenase is determined as described in Example 6.

It is known of the plant enzyme glutamate dehydrogenase that it reacts very sensitively to alterations in N supply.

Glutamate and 2-oxoglutarate exist in equilibrium and can be converted by transaminases or glutamate dehydrogenase.

It is possible that alanine aminotransferase (ALT), aspartate aminotransferase (AST), creatine kinase-muscle/brain (CK-MB), glutamate dehydrogenase (GLDH), or thyroxine may also show interference when sulfasalazine treatment is given at high doses.

The study director may choose to assess additional parameters in order to better characterise a test chemical’s toxicity (e.g. cholinesterase, lipids, hormones, acid/base balance, methaemoglobin or Heinz bodies, creatine kinase, myeloid/erythroid ratio, troponins, arterial blood gases, lactate dehydrogenase, sorbitol dehydrogenase, glutamate dehydrogenase, and gamma glutamyl transpeptidase).

The following list of parameters should be investigated (38): glucose, urea (urea nitrogen), creatinine, total protein, albumin, calcium, sodium, potassium, total cholesterol, at least two appropriate tests for hepatocellular evaluation (alanine aminotransferase, aspartate aminotransferase, glutamate dehydrogenase, total bile acids) (39), and at least two appropriate tests for hepatobiliary evaluation (alkaline phosphatase, gamma glutamyl transferase, 5’-nucleotidase, total bilirubin, total bile acids) (39).

Investigations of plasma or serum shall include sodium, potassium, glucose, total cholesterol, urea, creatinine, total protein and albumin, at least two enzymes indicative of hepatocellular effects (such as alanin aminotransferase, aspartate aminotransferase, alkaline phosphatase, ?-glutamyl trans-peptidase and glutamate dehydrogenase), and bile acids.

The study director may choose to assess additional parameters in order to better characterise a test chemical’s toxicity (e.g. cholinesterase, lipids, hormones, acid/base balance, methaemoglobin or Heinz bodies, creatine kinase, myeloid/erythroid ratio, troponins, arterial blood gases, lactate dehydrogenase, sorbital dehydrogenase, glutamate dehydrogenase, and gamma glutamyl transpeptidase).

Examples for components of this kind are substrates (for example alanine, aspartate, glutamate, pyruvate, 2-oxobutyrate, 2-oxoglutarate), auxiliary enzymes (for example malate dehydrogenase, lactate dehydrogenase, urease, glutamate dehydrogenase), other coenzymes such as adenosine diphosphate or adenosine triphosphate, or buffer substances that are common in enzymology, such as trishydroxymethylaminomethane-HCl and others as specified above.

A solution of 40 g/l of the agent obtained according to German Patent No. 11 55 134, 4.54 mmols/l of NADH2, 357 mmols/l of 2-oxoglutarate and 18 U/ml of glutamate dehydrogenase (GlDH) was lyophilized in glass bottles.

It does not show any influence on the activity of the enzymes which are commonly used as reagents or which are to be detected, for example alanine transaminase, aspartate transaminase, lactate dehydrogenase, glutamate dehydrogenase, malate dehydrogenase or urease.

Protein-saccharide conjugate of claim 1 wherein the protein is selected from the group consisting of hexokinase, glucose-6-phosphate dehydrogenase, cholesterol esterase, glucose oxidase, peroxidase, lactate dehydrogenase, glutamate dehydrogenase, creatine amidinohydrolase, creatine kinase, a-glucosidase, alkaline phosphatase, urokinase, cholesterol oxidase and sarcosine oxidase.

Glutamic acid was assayed as substrate and as compound of analogous structure in order to rule out the possibility that the described enzyme is a glutamate dehydrogenase.

However, also in many other important determination processes, such as the detection of aspartate transaminase, alanine transaminase, a-hydroxybutyrate dehydrogenase, creatine kinase, glutamate dehydrogenase, in the fully enzymatic urea determination, the enzymatic triglyceride determination or the glucose determination according to the hexokinase process, nicotinamide-adenine dinucleotide and/or nicotinamide-adenine-dinucleotide phosphate in the reduced and/or oxidized forms belong to the sensitive components which limit the period of utilization of the test package and whose stabilization is of great interest.

It has been mentioned initially that glutamate dehydrogenase reacts very sensitively to changes in the nitrogen supply, one example of this being a striking change in the ratio between the forward and reverse reactions of this enzyme.

The content of glutamate dehydrogenase is less than 0.01%, the content of L-malate dehydrogenase is less than 0.01% of the total activity.

The ammonia was determined on the one hand photometrically as indophenol and on the other hand enzymatically with the aid of glutamate dehydrogenase.

The enzymes in the form of nitrate reductase, glutamate dehydrogenase and pyruvate oxidase are each contained in a respective one of the chambers 8, 9 and 10, while reagents in the form of NADH, alpha-ketoglutarate and pyruvate are each filled into a respective one of the chambers 15, 16 and 17.

Preferred proteins are hexokinase, glucose-6-phosphate dehydrogenase, cholesterol esterase, glucose oxidase, peroxidase, lactate dehydrogenase, glutamate dehydrogenase, creatine amidinohydrolase, creatine kinase, a-glucosidase, alkaline phosphatase, urokinase, cholesterol oxidase or sarcosine oxidase.

Traditionally it was assumed that ammonium ions were assimilated into glutamic acid in the reaction catalysed by glutamate dehydrogenase.

In the case of pathological changes in the properties of cell membranes, it is to be expected that various pyridine-dependent dehydrogenases, such as lactate dehydrogenase (LDH), alcohol dehydrogenase (ADH), glyceraldehyde 3-phosphate dehydrogenase, isocitrate dehydrogenase, glutamate dehydrogenase, glucose dehydrogenase and glucose 6-phosphate dehydrogenase, and/or flavin-dependent dehydrogenases and/or flavin-dependent oxidases, such as succinate dehydrogenase, glycerol 3-phosphate dehydrogenase and glucose oxidase, pass into the serum and into other extracellular fluids, and that a threshold value pathological for the diagnosis is in each case found for each dehydrogenase or oxidase.

In the absence of glutamate dehydrogenase, we observed that the brain was no longer able to convert glutamate into energy, even though the amino acid was present in the brain," explains Melis Karaca, first author of this study.

In a further, preferred embodiment of the process according to the invention, therefore, the byproducts, such as, for example, reduction equivalents or amino group donors, which are generated by the enzymatic reactions of enzymes E and F are regenerated by using at least one enzyme G with amino acid dehydrogenase activity, such as, for example, alanine dehydrogenase, phenylalanine dehydrogenase, aspartate dehydrogenase and serine dehydrogenase, in particular glutamate dehydrogenase.