LDH

Lactate dehydrogenase (LDH) is an enzyme, consisting of five different isoenzymes, which catalyze the interconversion of L-lactate and pyruvate. LDH is present in the cytoplasm of all human tissues with higher concentrations in liver, heart and skeletal muscle and lower values in erythrocytes, pancreas, kidney and stomach. Increased LDH activities are found in a variety of pathological conditions such as myocardial infarction, cancer, diseases of liver, blood or muscle. However, because of the lack of organ specificity, determination of its isoenzymes or other enzymes such as alkaline phosphatase or ALAT/ASAT is necessary for differential diagnosis.

Optimized UV-test according to IFCC (International Federation of Clinical Chemistry and Laboratory Medicine)

N-Methyl-D-Glucamine L-Lactate

NAD+

• Reagent 1 contains sodium azide (0.95 g/L) as preservative. Do not swallow! • In very rare cases, samples of patients with gammopathy might give falsified results • Please refer to the safety data sheets and take the necessary precautions for the use of laboratory reagents.

340/410 nm (bichromatic)

Linear kinetics

Ascorbic acid Bilirubin (conjugated) Bilirubin (unconjugated) Lipemia Sulfapyridine Sulfasalazine Hemoglobin

0.0167

Female: < 247 U/L < 4.12 µkat/L Male: < 248 U/L < 4.14 µkat/L