The affinity of hemoglobin for oxygen is less than its structural analog myoglobin. However, this does not affect hemoglobin's usefulness for the body; on the contrary, it allows hemoglobin to be a more efficient carrier than myoglobin. This is because hemoglobin can release oxygen more easily than can myoglobin. It is both important for oxygen to be carried to different areas and also to be released when needed. The higher affinity of a given protein for oxygen, the harder it will be for that protein to release oxygen when needed. Therefore, hemoglobin's lower affinity for oxygen serves it well because it allows hemoglobin to release oxygen more easily in the body.
Answer:
The U.S. government protects fish, a common resource, by selling fishing licenses and regulating fish lengths
Explanation:
When there is regulation about a particular goods, it reduces the rate the availability of such goods is abused, US government could actually protect fish through licensing and regulation of the type to be sold including there length which ensures the protection of the juvenile.
No, because it still codes for valine in this case, but if another nucleotide was changed such as GCA it would code for alanine instead.
Answer:
It stores glucose that is taken from food so that respiration can happen later.
Here’s your answer, Enzymes !!
