Myoglobin

Myoglobin Human
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Description

Functional Roles

Myoglobin performs three primary roles:

  1. Oxygen Storage and Release: Binds O₂ with higher affinity than hemoglobin, enabling efficient extraction from hemoglobin and sustained release during hypoxia .

  2. Oxygen Diffusion Facilitation: Acts as a "shuttle" to enhance intracellular O₂ transport from capillaries to mitochondria .

  3. ROS Scavenging: Neutralizes reactive oxygen species (ROS) during oxidative stress .

Key Functional Data:

ParameterValue/Description
O₂ AffinityHigher than hemoglobin (P₅₀: ~2.8 mmHg vs. ~26 mmHg for hemoglobin) .
O₂ Binding KineticsRapid binding (on-rate: ~1.4 × 10⁶ M⁻¹s⁻¹) and slower release (off-rate: ~11 s⁻¹) .
NO ScavengingBinds nitric oxide (NO), regulating vascular tone and oxidative stress .

Clinical and Diagnostic Significance

Elevated serum myoglobin levels (>150 ng/mL) indicate muscle injury, such as rhabdomyolysis or myocardial infarction . A 2023 retrospective study of 6,872 critically ill patients revealed:

Myoglobin LevelProportionIn-Hospital MortalityKey Findings
<150 ng/mL43.5%12.5%Low mortality, stable trajectory .
150–499 ng/mL24.9%18.5%Mild elevation, moderate risk.
500–999 ng/mL19.6%25.3%Moderate elevation, higher risk.
≥1,000 ng/mL12.0%74.5%Severe elevation, poor prognosis .

Dynamic Monitoring Insights:

  • Rapidly rising myoglobin levels (e.g., ≥1,000 μg/mL) correlate with sepsis (59.6% prevalence), high SOFA scores (median 10), and reduced 28-day survival .

  • Trajectory modeling identifies four patient groups: steady, gradually decreasing, slowly rising, and rapidly rising, with survival time inversely proportional to myoglobin elevation rate .

Comparative Analysis with Hemoglobin

Myoglobin and hemoglobin share structural similarities but differ functionally:

FeatureMyoglobinHemoglobin
Subunits1 (monomer)4 (tetramer: 2 α, 2 β chains)
O₂ Capacity1 O₂ molecule4 O₂ molecules
Tissue LocalizationMuscles (cardiac, skeletal)Red blood cells
O₂ AffinityHigh (P₅₀: ~2.8 mmHg)Low (P₅₀: ~26 mmHg)
Primary RoleStorage and diffusionTransport

Emerging Research and Applications

Recent studies highlight novel roles:

  • Adaptive Functions: Myoglobin-deficient mice exhibit mitochondrial adaptations and enhanced NO signaling .

  • Diagnostics: Myoglobin serves as a prognostic marker in COVID-19 and sepsis, outperforming troponin in some contexts .

  • Food Science: Myoglobin oxidation affects meat color; additives like nitrite preserve its red hue .

Product Specs

Introduction
Myoglobin, a member of the globin superfamily found in skeletal and cardiac muscles, is a haemoprotein vital for intracellular oxygen storage and transcellular oxygen diffusion. This single-chain globular protein, composed of 153 amino acids, contains a heme prosthetic group (iron-containing porphyrin) at its core. With 8 alpha helices and a hydrophobic core, myoglobin exhibits a molecular weight of 16.7 kDa and serves as the primary oxygen-carrying pigment in muscle tissues. Unlike the cooperative oxygen binding observed in hemoglobin, myoglobin's oxygen binding is independent of surrounding oxygen pressure. Its hyperbolic oxygen dissociation curve reflects its rapid oxygen binding affinity. High myoglobin concentrations in muscle cells contribute to extended breath-holding capabilities in various organisms. Myoglobin plays a role in meat pigmentation, with color influenced by the iron atom's charge and attached oxygen. Primarily found in Type I, Type II A, and Type II B muscle fibers, myoglobin is generally absent in smooth muscle. Rhabdomyolysis, characterized by damaged muscle tissue, releases significant myoglobin, which, despite being filtered by kidneys, can induce acute renal failure due to its toxicity to renal tubular epithelium.
Description
This product consists of Human Myoglobin, produced from Human Cardiac Tissues, with a molecular mass of 17.5kDa. A key characteristic of Myoglobin is its rapid release from damaged myocardial cells following infarction, reaching peak levels faster than CK-MB or Troponin complex.
Physical Appearance
A sterile, red solution, filtered for purity.
Formulation
The protein is supplied in a solution of 0.05M phosphate buffer at pH 7.5, containing 0.15M NaCl and 0.09% NaN3. The solution has been sterile filtered through a 0.2µM membrane.
Stability
To ensure optimal stability, Human Myoglobin should be stored at a temperature of 2-8°C.
Purity
The purity level of this product is greater than 96.0%.
Human Virus Test

The starting material, obtained from the donor, has undergone rigorous testing and is certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.

Synonyms
Myoglobin, MB, PVALB, MGC13548.
Source
Human Cardiac Tissues.

Product Science Overview

Structure and Function

Myoglobin is structurally similar to hemoglobin, the oxygen-binding protein found in red blood cells. Both proteins contain a heme group, which is responsible for their ability to bind oxygen. The heme group contains an iron atom that can reversibly bind to an oxygen molecule. This binding imparts a red-brown color to the protein, contributing to the characteristic color of muscle tissue .

Unlike hemoglobin, which has a quaternary structure consisting of four subunits, myoglobin is a monomeric protein. This means it consists of a single polypeptide chain. Myoglobin’s primary function is to store oxygen and facilitate its transport from the cell membrane to the mitochondria, where it is used for aerobic respiration .

Discovery and Historical Significance

Myoglobin was the first protein to have its three-dimensional structure determined by X-ray crystallography. This groundbreaking work was conducted by John Kendrew, who received a share of the Nobel Prize in Chemistry in 1962 for his contributions. The elucidation of myoglobin’s structure provided significant insights into protein folding and function, marking a milestone in the field of structural biology .

Physiological Role

In humans, myoglobin is found in high concentrations in the heart and skeletal muscles. It is particularly abundant in Type I (slow-twitch) muscle fibers, which are adapted for endurance activities and rely heavily on aerobic metabolism. Myoglobin’s ability to bind and release oxygen efficiently makes it essential for maintaining oxygen supply during sustained muscle activity .

Myoglobin also plays a critical role in diving mammals, such as whales and seals, which have high concentrations of myoglobin in their muscles. This adaptation allows them to store large amounts of oxygen and remain submerged for extended periods .

Clinical Relevance

Myoglobin is released into the bloodstream following muscle injury, such as in cases of myocardial infarction (heart attack) or rhabdomyolysis (severe muscle breakdown). Elevated levels of myoglobin in the blood can be detected through laboratory tests and are used as a diagnostic marker for these conditions .

However, excessive myoglobin in the bloodstream can be harmful, as it can lead to kidney damage. This condition, known as myoglobinuria, occurs when myoglobin is filtered by the kidneys and precipitates in the renal tubules, causing obstruction and renal failure .

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