Let me share with you a difference between hemoglobin and myoglobin.
| Aspect | Hemoglobin | Myoglobin |
| Introduction | A type of protein found in red blood cells which are known as erythrocytes. | A type of protein presents in muscles fibers. |
| Function | Hemoglobin transports oxygen from the lungs to tissues and organs. | Myoglobin stores and releases oxygen within muscle cells. |
| Oxygen binding sites | Four heme groups, each with one iron atom | One heme group, also with one iron atom |
| Oxygen affinity | Cooperative binding, exhibits sigmoidal oxygen dissociation curve | Higher affinity for oxygen, exhibits a hyperbolic oxygen dissociation curve |
| Affinity for CO2 | Binds and transports carbon dioxide in the blood | Less effective in binding and transporting carbon dioxide |
| Structure | Tetrameric structure (composed of four subunits) | Monomeric structure (single polypeptide chain) |
| Size | Larger protein with molecular weight around 64 kDa | Smaller protein with molecular weight around 17 kDa |
| Regulation by pH | Undergoes Bohr effect, influenced by pH changes in blood | Less affected by pH changes in muscle tissues |
| Storage of oxygen | Does not store oxygen but facilitates its transport | Serves as an oxygen reservoir within muscle cells |
| Color | Gives red color to blood when oxygenated | Contributes to the reddish-brown color of muscles |
| Releases oxygen | Releases oxygen in tissues where oxygen levels are low | Releases oxygen in muscles during periods of increased demand |