yes
keratinThe correct answer is NOT keratin... the correct answer is myoglobin. This is the oxygen-binding pigment in muscle.
In cardiac disorders, myoglobin levels in the blood may increase due to damage to heart muscle cells. Elevated myoglobin levels can indicate myocardial infarction (heart attack) or other types of cardiac injury. Myoglobin is released into the blood when heart muscle cells are damaged, making it a useful biomarker for detecting and monitoring cardiac disorders.
Nitric oxide myoglobin is a form of myoglobin that can bind to nitric oxide. This interaction helps regulate blood flow by releasing nitric oxide, which acts as a vasodilator to increase blood vessel diameter and improve oxygen delivery to tissues.
Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is the iron- and oxygen-binding protein in blood, specifically in the red blood cells. The only time myoglobin is found in the bloodstream is when it is released following muscle injury. It is an abnormal finding, and can be diagnostically relevant when found in blood. For full information about myoglobin see the related link below.
You have a myoglobin, an oxygen storage molecule akin to haemoglobin, in the blood. This could be due to the muscle trauma or ischaemia leading to death and breakdown. Myoglobin is toxic to kidney nephrons.
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.
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.
Plasma
Plasma and water.
Hemoglobin is a protein in red blood cells that carries oxygen from the lungs to the rest of the body, while myoglobin is a protein found in muscle cells that stores oxygen for muscle use. Hemoglobin has a higher oxygen affinity and is responsible for transporting oxygen, whereas myoglobin releases oxygen for muscle metabolism when needed.
Myoglobin levels can rise in hypothyroidism due to decreased muscle metabolism and increased muscle injury or damage. Hypothyroidism often leads to muscle weakness and atrophy, which may release myoglobin into the bloodstream. Additionally, altered muscle blood flow and changes in the expression of proteins involved in muscle repair can contribute to elevated myoglobin levels. Overall, the metabolic and physiological changes associated with hypothyroidism can lead to increased leakage of myoglobin from muscle tissues.
Myoglobin has a very high affinity for oxygen, meaning it binds it very strongly. At very low oxygen concentrations in the cell, myoglobin releases its oxygen, despite the high affinity, simply because there are too few oxygen molecules around to rebind to the myoglobin when they are released naturally from the myoglobin (which usually occurs anyway). Once the oxygen concentration increases again, returning to normal, oxygen molecules will collide with myoglobin. The myoglobin, with its high oxygen affinity, will strongly bind any oxygen that meets it, replenishing myoglobin's oxygen storage very quickly. As myoglobin's affinity for oxygen is stronger the haemoglobin's, it will 'steal' oxygen from haemoglobin in the blood very easily, replacing its bound oxygen. This binding system serves to release oxygen when it is needed if blood oxygen levels are reduced (due to high levels of exercise), but replenishes the supply when oxygen levels begin to rise again.