Oxygen Binding and Hemoglobin Function

The video explains the oxygen hemoglobin dissociation curve, a key concept in understanding how oxygen is transported in the blood. It covers the structure and function of hemoglobin, the significance of the dissociation curve, and factors that affect it, such as pH, carbon dioxide levels, and temperature. The video also discusses the Bohr effect and the role of 2-3 diphosphoglycerate in shifting the curve. The content is designed for quick study and review, providing a comprehensive overview of these essential physiological processes.

What is the primary purpose of respiration?

• To produce energy

• To regulate temperature

• To circulate blood

• To exchange gases

What percentage of oxygen in the blood is bound to hemoglobin?

• 98%

• 75%

• 50%

• 2%

How many oxygen molecules can one hemoglobin molecule bind?

• Four

• One

• Two

• Three

What shape is the oxygen hemoglobin dissociation curve?

• Parabolic

• Sigmoidal

• Linear

• Exponential

What happens to the oxygen hemoglobin dissociation curve when the pH decreases?

• Shifts to the left

• Shifts to the right

• Becomes parabolic

• Becomes linear

Which factor does NOT shift the oxygen dissociation curve to the right?

• High 2-3 DPG

• Low pH

• Low temperature

• High pCO2

What is the Bohr effect?

• Increased oxygen binding at high altitudes

• Decreased oxygen binding due to high temperature

• Increased oxygen affinity in fetal hemoglobin

• Decreased oxygen affinity due to carbon dioxide binding

How does 2-3 DPG affect oxygen binding to hemoglobin?

• Increases affinity

• Decreases affinity

• Has no effect

• Binds directly to oxygen

What is a characteristic of fetal hemoglobin compared to adult hemoglobin?

• No oxygen affinity

• Lower oxygen affinity

• Same oxygen affinity

• Higher oxygen affinity

Which chains are present in fetal hemoglobin?

• Two alpha and two beta

• Two alpha and two gamma

• Two beta and two gamma

• Two delta and two gamma