Log in
Biochemistry · Additional topics

Blood lactate dehydrogenase

Lactate dehydrogenase

Lactate dehydrogenase (LDH) is an intracellular cytosolic enzyme that catalyzes the reversible conversion of pyruvate to lactate. Normally, it is present in blood plasma in trace amounts, but upon cell membrane damage or tissue necrosis, it massively enters the bloodstream, serving as a critical indicator of a pathological process.

Serum reference range55–140 IU/L
ReactionPyruvate + NADH₂ ↔ lactate + NAD⁺
Isoenzymes5 isoforms (LDH-1 – LDH-5) composed of H and M subunits
Dynamics in myocardial infarctionActivity increases after 24–48 hours
LocalizationCell cytosol
4 min readFor medical studentsUpdated 10.10.2026
Material prepared by WhiteCoat Pro editorial team based on platform study guidesPending instructor review

LDH in enzymodiagnostics

Enzymodiagnostics is a method for detecting diseases and assessing their severity based on measuring enzyme activity in biological fluids. The main goal of this approach is to establish the precise localization of the pathological process, its stage, and treatment efficacy.

All blood plasma enzymes by origin are divided into three large groups:

  1. Secretory. Synthesized by cells and purposefully secreted into plasma, where they perform their primary function (e.g., blood coagulation factors).
  2. Excretory. Produced in exocrine glands and secreted into the GI lumen to aid digestion. They enter the blood only when glands are damaged (e.g., amylase and lipase in pancreatitis).
  3. Cellular (indicator). Lactate dehydrogenase belongs to this group. These proteins function exclusively inside cells. Normally, their plasma activity is consistently low and results solely from natural cell death and tissue turnover. However, upon cytolysis (membrane destruction) or deep necrosis, a significant release of enzymes occurs, leading to a manifold increase in their blood activity.

LDH isoenzymes and their tissue distribution

The appearance of the cytosolic enzyme LDH in plasma indicates increased cell membrane permeability. However, total enzyme activity does not accurately identify which specific organ has been damaged. To solve this problem, isoenzyme spectrum analysis is used.

Isoenzymes (isozymes) are multiple molecular forms of the same enzyme. They catalyze the exact same reaction but differ in structure, physicochemical properties (specifically, electrophoretic mobility), and, most importantly, tissue representation.

The lactate dehydrogenase molecule consists of two types of subunits: H (heart) and M (muscle). Their various combinations form five isoforms, which are separated by plasma electrophoresis:

  • LDH-1 and LDH-2 — most active in the heart muscle and kidneys.
  • LDH-4 and LDH-5 — predominate in skeletal muscles and the liver.
  • Other variants are present in remaining tissues in various proportions.
Test your knowledge on this topicTasks from the Biochemistry course bank — instant answer and detailed explanation.

Diagnostic interpretation of the LDH spectrum

Determining the isoenzyme spectrum allows not only to establish the fact of tissue damage but also to localize the affected organ. This is a key advantage of isoenzyme analysis over measuring total nonspecific enzyme activity. The normal range of total LDH activity in serum is $55\text{--}140$ IU/L.

A healthy individual exhibits a physiological distribution of isoforms without a pronounced shift in either direction. When pathology develops, the electrophoretic pattern changes:

ConditionChange in LDH spectrumShift characteristics
Myocardial infarctionSharp increase in LDH-1 and LDH-2 levels"Left shift of the spectrum"
HepatitisIncreased LDH-5 level"Right shift of the spectrum"
Skeletal muscle damageIncreased LDH-4 and LDH-5 levels"Right shift of the spectrum"

Thus, plasma electrophoresis is performed for the differential diagnosis of heart, liver, and skeletal muscle diseases. For example, in myocardial infarction, LDH activity (due to the LDH-1 fraction) begins to rise $24\text{--}48$ hours after the attack. In poisonings with organochlorine compounds or viral hepatitis, an increase in "hepatic" fractions is observed.

How to memorize

Remembering the distribution of LDH isoenzymes is facilitated by a numerical association: "one" (LDH-1) is the body's main motor (the heart), while "five" (LDH-5) corresponds to the five lobes of the liver. Accordingly, a shift of the spectrum toward the beginning (left) indicates an infarction, while a shift toward the end (right) indicates hepatitis.

Class and exam questions

Why is it important to determine LDH isoenzymes rather than just total activity in myocardial infarction?

An increase in total LDH activity is nonspecific and may be associated with damage to various organs. Isolating the LDH-1 and LDH-2 fractions allows for precise localization of necrosis in the heart muscle, ruling out liver or skeletal muscle pathology.

How soon after a myocardial infarction does LDH appear in the blood?

LDH reacts relatively late: its level begins to rise 24–48 hours after myocardial damage. For earlier diagnosis, other indicator enzymes are used, such as creatine phosphokinase (CK), which rises as early as 3–6 hours.

What does the appearance of cytosolic and mitochondrial enzymes in plasma indicate?

The release of cytosolic enzymes (which include LDH) into the blood indicates reversible increased permeability of cell membranes. The appearance of mitochondrial enzymes (e.g., m-AST), on the other hand, indicates deep necrosis and organelle destruction.

Got questions? Ask the AIThe AI tutor has read the material on "Blood lactate dehydrogenase" and will explain it in simple terms.

What else to study on this topic

  • Creatine phosphokinase (CK) and the diagnostic significance of the CK-MB fraction
  • Aminotransferases (ALT and AST) as markers of liver and heart pathologies
  • De Ritis ratio: calculation and clinical interpretation
  • Excretory blood plasma enzymes (amylase, lipase, trypsin)
  • Differences between organ-specific and organelle-specific enzymes

Master the entire topic in the "Biochemistry" course

This is a summary. The course covers everything tested in classes and exams.

  • Complete study guide on "Blood lactate dehydrogenase" and 3,616 other subject pages
  • Assignments and quizzes after every topic — just like in a colloquium
  • AI tutor answers questions on the topic anytime
  • 115 video lessons on the subject

Other topics in the "Additional Topics" section

Free video lessons: biochemistryShort lessons with study notes — no registration required.

Watch lessons

Prepared by WhiteCoat Pro faculty in accordance with the medical school curriculum. For educational purposes only.