What is Lactate Dehydrogenase (LDH)? Lactate Dehydrogenase (LDH) is an enzyme found in nearly all body tissues, particularly in the heart, liver, kidneys, muscles, and red blood cells. It catalyzes the conversion of lactate to pyruvate, playing a key role in energy metabolism. Measuring serum LDH levels is used to detect tissue damage, monitor diseases such as myocardial infarction, liver disease, or malignancies, and assess conditions involving hemolysis or inflammation. LDH exists in five isoenzymes (LDH-1 to LDH-5), which can provide additional diagnostic specificity.
Definition: The LDH Unit Converter converts serum LDH activity between various units, enabling standardization of laboratory results for clinical use.
Purpose: It assists clinicians and researchers in interpreting LDH levels across different measurement units (e.g., µkat/L to IU/L), ensuring accurate diagnosis and monitoring of conditions associated with tissue damage or disease.
Converting LDH activity between units is critical for:
Elevated Levels: High LDH levels (e.g., >250 IU/L or >4.17 µkat/L in adults) may indicate:
Low Levels: Low LDH levels are rare and typically not clinically significant, as LDH is ubiquitous in tissues. They may reflect:
Normal Ranges:
Interferences:
Q: Why are there different units for LDH?
A: Different units reflect varying standards; µkat/L and nkat/L are SI units, while IU/L and U/L are commonly used in clinical practice for enzyme activity measurements.
Q: What is a normal LDH level?
A: Normal LDH is typically 120–250 IU/L (2.0–4.17 µkat/L) in adults, varying by age and lab. Consult a healthcare provider for interpretation.
Q: Can this converter be used for other enzymes?
A: No, this converter is specific to LDH; other enzymes (e.g., AST, ALT) have different activity measurements and conversion factors—consult a healthcare provider for accuracy.