myglobin
keratinThe correct answer is NOT keratin... the correct answer is myoglobin. This is the oxygen-binding pigment in muscle.
Myoglobin's function is similar to that of hemoglobin, which carries oxygen in red blood cells to various tissues. Myoglobin has even higher affinity for oxygen than hemoglobin and is specific to muscle cells. Myoglobin thus acts as a storage of oxygen, as it holds oxygen inside heart and skeletal muscles.
Myoglobin-myoglobin stores oxygen from red blood cells, which are red. The reason myoglobin stores oxygen (if you wanna know) is to have it available when there's muscle activity.
Basically it binds with oxygen to form oxymyoglobin. when muscles are excercising excessively oxymyoglobin splits and the oxygen is released into the blood to fuel the muscles by assisting in the production of ATP. The main function of myoglobin is to carry oxygen to muscle tissues that have been damaged. Myoglobin is only found in a muscle injury.
Myoglobin is synthesized in muscle cells and imparts the reddish-brown color of skeletal muscle tissue. Like hemoglobin, myoglobin can combine loosely with oxygen. This ability to temporarily store oxygen reduces a muscle's requirement for a continuous blood supply during muscular contraction.
hemoglobin like compound that stores oxygen in muscles
Myoglobin is synthesized in cells and imparts the reddish-brown color of skeletal muscle tissue. Like hemoglobin, myoglobin can combine loosely with oxygen. This ability to temporarily store oxygen reduces a muscle's requirement for a continuous blood supply during muscular contraction.
connective tissues stores fats in the body
Both Myoglobin and Haemoglobin binds to oxygen, but they differ in many aspects. Usual site: Myoglobin: muscle tissues Haemoblogin: red blood cells (whole body) Main function: Myoglobin: stores oxygen (in muscle tissues) Haemoglobin: Oxygenation of tissues (whole body) Waste (CO2) collection (whole body) gas exchange (lungs, tissues) Oxygen carrying capacity: Myoglobin: monomeric = one heme prosthetic group, one iron atom Haemoglobin: tetrameric = four heme prosthetic groups, four iron atoms. Structure Myoglobin: secondary and tertiary, no allosteric interaction Haemoglobin: quaternary structure, allosteric interaction, different affinity Affinity to oxygen Myoglobin: Oxidation (Fe2+ → Fe3+) prevents oxygen binding. Haemoglobin: requirement specific affinity: (gradually increasing in the lungs, . gradually decreasing at the tissues) Prefered binding Myoglobin: Carbon monoxide preferred to Oxygen. Haemoglobin: Oxygen, carbon dioxide While in cases of hugely increased demand, myoglobin releases oxygen for metabolism, but, in the long run haemoglobin is more suitable for the purpose.
myoglobin
Cells that do a lot of work or activity such as muscle cells.
Because your body is still trying to replenish ATP, muscle glygogen and blood oxygen stores/levels to before exercise levels. Its commonly referred to as EPOC or excess post oxygen consumoption.