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Serum Myoglobin Test – Indications, Procedures, Results

Last updated: February 8, 2026 Medically reviewed by: RxHarun Orthopedic Specialist Doctor Reading time: 8 min read

A serum myoglobin test is used to measure the level of myoglobin in your blood and it is a protein that’s typically found in the heart and skeletal muscle tissues. The only time that myoglobin is found in the bloodstream is when an injury to a muscle has occurred. The myoglobin blood test measures the level of the protein myoglobin in the blood. Myoglobin can also be measured with a urine test.

How the Test is Performed

A blood sample is needed.

How to Prepare for the Test

No special preparation is needed.

How the Test will Feel

When the needle is inserted to draw blood, some people feel moderate pain. Others feel only a prick or stinging. Afterward, there may be some throbbing or a slight bruise. This soon goes away.

Why the Test is Performed

Myoglobin is a protein in the heart and skeletal muscles. When you exercise, your muscles use up available oxygen. Myoglobin has oxygen attached to it, which provides extra oxygen for the muscles to keep at a high level of activity for a longer period.

When a muscle is damaged, myoglobin in muscle cells is released into the bloodstream. The kidneys help remove myoglobin from the blood into the urine. When the level of myoglobin is too high, it can damage the kidneys.

This test is ordered when your health care provider suspects you have muscle damage, such as of the heart or skeletal muscle.

Normal Results

The normal range is 0 to 85 ng/mL.

Note: Normal value ranges may vary slightly among different laboratories. Some labs use different measurements or may test different samples. Talk to your doctor about the meaning of your specific test results.

What Abnormal Results Mean

An increased level of myoglobin may be due to:

  • Heart attack
  • Malignant hyperthermia (very rare)
  • Muscular dystrophy
  • Breakdown of muscle tissue that leads to the release of muscle fiber contents into the blood ( rhabdomyolysis )
  • Skeletal muscle inflammation ( myositis )
  • Skeletal muscle ischemia (oxygen deficiency)
  • Skeletal muscle trauma

Risks

There is very little risk involved with having your blood taken. Veins and arteries vary in size from one patient to another, and from one side of the body to the other. Taking blood from some people may be more difficult than from others.

Other risks associated with having blood drawn are slight, but may include:

  • Excessive bleeding
  • Fainting or feeling lightheaded
  • Hematoma (blood accumulating under the skin)
  • Infection (a slight risk any time the skin is broken)

FAQ

What is the normal range for myoglobin?

Normal Results
  • The normal range is 25 to 72 ng/mL (1.28 to 3.67 nmol/L). Note: Normal value ranges may vary slightly among different laboratories. Some labs use different measurements or may test different samples. Talk to your provider about the meaning of your specific test results.

What does low myoglobin in blood tests mean?

  • Lower results may mean you have: Rheumatoid arthritis. Myasthenia gravis. Antibodies to myoglobin in your blood.

What is the difference between myoglobin and hemoglobin?

  • Hemoglobin is a heterotetrameric oxygen transport protein found in red blood cells (erythrocytes), whereas myoglobin is a monomeric protein found mainly in muscle tissue where it serves as an intracellular storage site for oxygen.

What is the main function of myoglobin?

  • myoglobin, a protein found in the muscle cells of animals. It functions as an oxygen-storage unit, providing oxygen to the working muscles.

What causes myoglobin levels to rise?

  • Increased myoglobin levels can occur after muscle injections or strenuous exercise. Because the kidneys remove myoglobin from the blood, the myoglobin level may be high in people whose kidneys are failing. Heavy alcohol consumption and certain drugs can also cause muscle injury and increase myoglobin in the blood.

How do you treat myoglobin?

  • Getting enough fluid into your body is the first and most important treatment. A healthcare professional must start administering IV fluids quickly. This fluid should contain bicarbonate, which helps flush the myoglobin out of your kidneys.

How do I lower myoglobin levels?

  • Raising the pH of the urine to 6.5 or more can be facilitated by adding sodium bicarbonate to the fluids. Alkalinization of the urine has been postulated to minimize the breakdown of myoglobin into its nephrotoxic metabolites and to reduce the crystallization of uric acid, thereby decreasing damage to tubule cells.

Is myoglobin positive or negative charge?

  • Myoglobin retains a total net charge of +26.6 at pH 3.5 and a total net negative charge of −7.3 at pH 7.4 (calculated through PROTEIN CALCULATOR v3. 3 software).

Is hemoglobin better than myoglobin?

  • Our body prefers to use hemoglobin rather than myoglobin as the oxygen carrier in the bloodstream. This is because hemoglobin not only binds oxygen weakly but more importantly binds oxygen cooperatively.

What are the 4 subunits of hemoglobin?

  • Hemoglobin is made up of four polypeptide subunits, two alpha (α) subunits, and two betas (β) subunits. Each of the four subunits contains a heme ( contains iron) molecule, where the oxygen itself is bound through a reversible reaction, meaning that a hemoglobin molecule can transport four oxygen molecules at a time.

Is myoglobin in urine normal?

  • Normal Results
  • A normal urine sample does not have myoglobin. A normal result is sometimes reported as negative. Normal value ranges may vary slightly among different laboratories. Talk to your provider about the meaning of your specific test results.

Is myoglobin acidic or basic?

  • It is not the myoglobin itself that is toxic (it is a protoxin) but the ferrihemate portion that is dissociated from myoglobin in acidic environments (e.g., acidic urine, lysosomes). Myoglobin is a sensitive marker for muscle injury, making it a potential marker for heart attack in patients with chest pain.

What are the two types of hemoglobin?

  • Normal hemoglobin types include Hemoglobin A: which makes up about 95%-98% of Hb found in adults; it contains two alpha and two beta protein chains. Hemoglobin A2: makes up about 2%-3% of Hb in adults; it has two alpha and two delta protein chains.Nov 9, 2021

What kind of protein is in myoglobin?

  • Globular protein, Myoglobin (Mb) is a heme-containing globular protein that is found in abundance in myocyte cells of heart and skeletal muscle.

What amino acids are in myoglobin?

  • Myoglobin is generally found in muscle tissues of vertebrates. It consists of a single polypeptide chain of 153 amino acids called globin.

What do Myofibrils do?

  • The main function of myofibrils is to perform muscle contraction. There is an incomplete overlap between the thin and the thick filaments when the muscle is at rest.

Is myoglobin a fibrous protein?

  • Globular proteins are spherical in shape and consist of long chains with numerous branches and offshoots which make them great as transport proteins. Examples of fibrous proteins are collagen, elastin, keratin, silk, etc. Examples of globular proteins are myoglobin, hemoglobin, casein, insulin, etc.

Is myoglobin an enzyme?

  • Myoglobin has also been shown to have enzymatic functions. It is necessary for the decomposition of bioactive nitric oxide to nitrate.

What is a normal myoglobin level?

  • The normal range is 25 to 72 ng/mL (1.28 to 3.67 nmol/L). Note: Normal value ranges may vary slightly among different laboratories. Some labs use different measurements or may test different samples.

What is the main function of myoglobin?

  • Myoglobin is a protein that’s found in your striated muscles, which include skeletal muscles (the muscles attached to your bones and tendons) and heart muscles. Its main function is to supply oxygen to the cells in your muscles (myocytes).

What is the biological function of myoglobin?

  • Myoglobin, a protein found in the muscle cells of animals. It functions as an oxygen-storage unit, providing oxygen to the working muscles. Diving mammals such as seals and whales are able to remain submerged for long periods because they have greater amounts of myoglobin in their muscles than other animals do.

How do you treat myoglobin?

  • Getting enough fluid into your body is the first and most important treatment. A healthcare professional must start administering IV fluids quickly. This fluid should contain bicarbonate, which helps flush the myoglobin out of your kidneys.

What Causes High Amounts of Myoglobin?

  • Rhabdomyolysis. Rhabdomyolysis is a condition that causes muscle damage and muscle death.
  • Severe muscle injury.
  • Heart attack.
  • Malignant hyperthermia.
  • Muscular dystrophy.
  • A muscular dystrophy is a group of diseases that leads to muscle weakness. …
  • Myositis.

How do I lower myoglobin levels?

  • Raising the pH of the urine to 6.5 or more can be facilitated by adding sodium bicarbonate to the fluids. Alkalinization of the urine has been postulated to minimize the breakdown of myoglobin into its nephrotoxic metabolites and to reduce the crystallization of uric acid, thereby decreasing damage to tubule cells.

What color is myoglobin in urine?

  • Myoglobinuria is brown, and often only a few RBCs are present in the urine. Hematuria produces reddish sediment in spun urine samples. Red or brown urine with a negative dipstick result for blood indicates a dye in the urine.

Is myoglobin in urine normal?

  • Normal Results
  • A normal urine sample does not have myoglobin. A normal result is sometimes reported as negative. Normal value ranges may vary slightly among different laboratories. Talk to your provider about the meaning of your specific test results.

How do you differentiate between positive test results of myoglobin and blood?

  • Generally, to differentiate myoglobinuria from hemoglobinuria and hematuria, which all have a positive blood test on a urine dipstick, evaluate the color of the supernatant after centrifugation of the urine; hematuria will have a clear supernatant, whereas hemoglobinuria and myoglobinuria will not.

What is the function of myoglobin and hemoglobin?

  • Hemoglobin functions as an oxygen carrier from the lungs to the entire body and myoglobin functions as a storer of oxygen in the muscle cells.

Frequently Asked Questions

Is this article a replacement for a doctor?

No. It is educational content only. Patients should consult a qualified clinician for diagnosis and treatment.

When should I seek urgent care?

Seek urgent care for severe symptoms, rapidly worsening condition, breathing difficulty, severe pain, neurological changes, or any emergency warning sign.

References

Add references, clinical guidelines, textbooks, journal articles, or trusted medical sources here. You can edit this area later with a custom field named _rx_references.

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Written by Dr. Harun Ar Rashid, MD - Arthritis, Bones, Joints Pain, Trauma, and Internal Medicine Specialist

Dr. Md. Harun Ar Rashid, MPH, MD, PhD, is a highly respected medical specialist celebrated for his exceptional clinical expertise and unwavering commitment to patient care. With advanced qualifications including MPH, MD, and PhD, he integrates cutting-edge research with a compassionate approach to medicine, ensuring that every patient receives personalized and effective treatment. His extensive training and hands-on experience enable him to diagnose complex conditions accurately and develop innovative treatment strategies tailored to individual needs. In addition to his clinical practice, Dr. Harun Ar Rashid is dedicated to medical education and research, writing and inventory creative thinking, innovative idea, critical care managementing make in his community to outreach, often participating in initiatives that promote health awareness and advance medical knowledge. His career is a testament to the high standards represented by his credentials, and he continues to contribute significantly to his field, driving improvements in both patient outcomes and healthcare practices. Born and educated in Bangladesh, Dr. Rashid earned his BPT from the University of Dhaka before pursuing postgraduate training internationally. He completed his MD in Internal Medicine at King’s College London, where he developed a special interest in inflammatory arthritis and metabolic bone disease. He then undertook a PhD in Orthopedic Science at the University of Oxford, conducting pioneering research on cytokine signaling pathways in rheumatoid arthritis. Following his doctoral studies, Dr. Rashid returned to clinical work with a fellowship in interventional pain management at the Rx University School of Medicine, refining his skills in image-guided joint injections and minimally invasive pain-relief techniques.