Myoglobin can be separated from hemoglobin by saturating the specimen with which reagent?

Myoglobin can be effectively separated from hemoglobin by saturating the specimen with ammonium sulfate. This reagent is commonly used in protein purification processes because it induces protein precipitation in a controlled manner. By increasing the concentration of ammonium sulfate in the solution, proteins such as myoglobin and hemoglobin undergo changes in solubility, allowing for their separation based on their differing isoelectric points and solubilities in varying concentrations of ammonium sulfate.

In contexts like this, separating myoglobin from hemoglobin is important for various diagnostic purposes, particularly in assessing muscle injury, as myoglobin release in higher quantities can indicate muscle damage while hemoglobin is integral to oxygen transport in the blood. The use of ammonium sulfate leverages the principle of salting out, where proteins are separated based on their solubility changes in the presence of salts.