All of the following statements are true except 2,3-bisphosphoglycerate decreases the affinity of hemoglobin for oxygen. hemoglobin will bind more oxygen when the partial pressure is low than when the partial pressure is high. oxygen dissociates more readily from hemoglobin as ph decreases. increased partial pressure of carbon dioxide increases oxygen dissociation from hemoglobin. decreasing temperature will cause a shift to the left in the hemoglobin saturation curve.

hemoglobin will bind more oxygen when the partial pressure is low than when the partial pressure is high.

Explanation:

Binding of hemoglobin to oxygen is regulated by several factors. However, the partial pressure of oxygen is the most important factor that determines how much oxygen will bind to hemoglobin. When the partial pressure of O2 is high, hemoglobin binds with large amounts of O2. On the other hand, when the partial pressure of O2 is low, hemoglobin is only partially saturated.

Therefore, the greater the partial pressure of oxygen, the more O2 will bind to hemoglobin until saturation is reached. This is why a lot of O2 binds to hemoglobin in pulmonary capillaries where the partial pressure of oxygen is high.

answer: glucoamylase presented optimum activity at temperature of 55â°c, and, in the glycosidic bonds from the non-reducing ends of starch, resulting in the production of glucose. source and type of fermentation can affect the enzyme's properties

credit to kalahira

after a the power stroke, adp is released, but the cross-bridge formed is still in place. atp then binds to myosin, moving the myosin to its high-energy state, releasing the myosin head from the actin active site.