LDH
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How many isoenzyme are in LDH?
5
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
Ldh are high in what organ
Liver, heart and skeletal muscle
Ldh are low in what organ
erythrocytes, pancreas, kidney and stomach.
Increased LDH activities
Myocardial infarction, cancer, disease of liver, blood or muscle
Method LDH
Optimized UV-test according to IFCC (International Federation of Clinical Chemistry and Laboratory Medicine) [ L lactate ➕ nad➕ ➡️pyruvate ➕NADH➕ H➕
Components and Concentrations LDH
R1: N-Methyl-D-Glucamine (ph8.4) 420 mmol/L L-Lactate 65 mmol/L R2: NAD➕ 50 mmol/L
Storage and Stability
Reagents are stable up to the date of expiry indicated on the kit, if stored at 2 – 8°C and contamination is avoided. Do not freeze reagents and protect them from light.
Warnings and precautions
• Reagent 1 contains sodium azide (0.95 g/L) as preservative. Do not swallow! Avoid contact with skin and mucous membranes. • In very rare cases, samples of patients with gammopathy might give falsified results [3]. • Please refer to the safety data sheets and take the necessary precautions for the use of laboratory reagents. For diagnostic purposes, the results should always be assessed with the patient’s medical history, clinical examinations and other findings.
Wavelength
340/410
Temp
37
Measuring range
43 U/L up to 1500 U/L
Limit of detection
15 U/L
Interfering substance
Ascorbic acid Conjugated bilirubin Unconjugated bilirubin Lipemis Sulfapryridine Sulfasalazine Hemoglobin
Conversion factor
0.0167
Reference range
W <247 U/L <4.12 ukat/L M > 248 U/L <4.14 ukat/L
Highest ldh are seen
Pernicious anemua and hemolytic disorders