<span>situated or extending across something.</span>
Answer:
c. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron.
e. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ( Fe ) (Fe) atom.
f. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. The heme prosthetic group is entirely buried within myoglobin.
Explanation:
The differences between hemoglobin and myoglobin are most important at the level of quaternary structure. Hemoglobin is a tetramer composed of two each of two types of closely related subunits, alpha and beta. Myoglobin is a monomer (so it doesn't have a quaternary structure at all). Myoglobin binds oxygen more tightly than does hemoglobin. This difference in binding energy reflects the movement of oxygen from the bloodstream to the cells, from hemoglobin to myoglobin.
Myoglobin binds oxygen
The binding of O 2 to myoglobin is a simple equilibrium reaction:
Answer:
Here's your Answer
Explanation:
the mass spectrum is the graphical representation of the ion abundance versus the mass to charge of the ions separated in mass spectrometer
Answer:
Cobalt Sources
Cobalt-60 is used as a radiation source in many common industrial applications, such as in leveling devices and thickness gauges. It is also used for radiation therapy in hospitals. Accidental exposures may occur as the result of loss or improper disposal of medical and industrial radiation sources.
Explanation:
