leghemoglobin is a protein found in muscle that can bind to and store oxygen.
a protein found in muscle that can bind to and store oxygen?
leghemoglobin
section::::other oxygen-binding proteins.









































bullet::::- myoglobin: found in the muscle tissue of many vertebrates, including humans, it gives muscle tissue a distinct red or dark gray color. it is very similar to hemoglobin in structure and sequence, but is not a tetramer; instead, it is a monomer that lacks cooperative binding. it is used to store oxygen rather than transport it.









































bullet::::- hemocyanin: the second most common oxygen-transporting protein found in nature, it is found in the blood of many arthropods and molluscs. uses copper prosthetic groups instead of iron heme groups and is blue in color when oxygenated.
hemoglobin
dystrophin is a large, rod-like cytoskeletal protein found at the inner surface of muscle fibers. dystrophin is missing in duchenne muscular dystrophy patients and is present in reduced amounts in becker muscular dystrophy patients. the protein encoded by this gene is a peripheral membrane protein found associated with dystrophin and dystrophin-related proteins. this gene is a member of the syntrophin gene family, which contains at least two other structurally related genes. the pdz domain of syntrophin-α1(snta1), the most abundant isoform in the heart, has been reported to bind to the c-terminal domain of murine cardiac voltage-gated sodium channels (skm2) causing altering ion channel activity leading to long qt syndrome.
syntrophin, alpha 1