Chapter 29, Problem 29.49AP

(a)

Interpretation Introduction

Interpretation:

The raising of temperature will cause haemoglobin to release more ${\text{O}}_{\text{2}}$ to the tissues or to absorb more ${\text{O}}_{\text{2}}$ has to be identified.

Concept Introduction:

Haemoglobin:

• Composed of four polypeptide chain with a quaternary structure.
• A central heme molecule is there in each protein chain and each of the four hemes can bind with one ${\text{O}}_{\text{2}}$ molecule.
• Each heme molecule in its centre has ${\text{Fe}}^{\text{+2}}$
• The bright red haemoglobin with four oxygens is called oxy haemoglobin.
• The dark red-purple haemoglobin in which one or more oxygen is lost is called deoxyhaemoglobin.

The degree of saturation of haemoglobin is the percentage of heme units bound to oxygen at a given moment.

The binding of $O_2$ to haemoglobin depends on the $p{O}_2$ (partial pressure of oxygen) in the blood and the bonding strength, or affinity between oxygen and haemoglobin. Oxygen diffuses out of the arterial ends of tissue capillaries and carbon dioxide out of the tissue because of difference in partial pressure.

The factors which depend on the release of $O_2$ to the tissues and absorption of oxygens are temperature, ${\text{H}}^{\text{+}}$ concentration and ${\text{CO}}_{\text{2}}$ concentration.

(b)

Interpretation Introduction

Interpretation:

The increased production of ${\text{CO}}_{\text{2}}$ will cause haemoglobin to release more ${\text{O}}_{\text{2}}$ to the tissues or to absorb more ${\text{O}}_{\text{2}}$ has to be identified.

Concept Introduction:

Haemoglobin:

• Composed of four polypeptide chain with a quaternary structure.
• A central heme molecule is there in each protein chain and each of the four hemes can bind with one ${\text{O}}_{\text{2}}$ molecule.
• Each heme molecule in its centre has ${\text{Fe}}^{\text{+2}}$
• The bright red haemoglobin with four oxygens is called oxy haemoglobin.
• The dark red-purple haemoglobin in which one or more oxygen is lost is called deoxyhaemoglobin.

The degree of saturation of haemoglobin is the percentage of heme units bound to oxygen at a given moment.

The binding of $O_2$ to haemoglobin depends on the $p{O}_2$ (partial pressure of oxygen) in the blood and the bonding strength, or affinity between oxygen and haemoglobin. Oxygen diffuses out of the arterial ends of tissue capillaries and carbon dioxide out of the tissue because of difference in partial pressure.

The factors which depend on the release of $O_2$ to the tissues and absorption of oxygens are temperature, ${\text{H}}^{\text{+}}$ concentration and ${\text{CO}}_{\text{2}}$ concentration.

(c)

Interpretation Introduction

Interpretation:

The increased production of ${\text{H}}^{\text{+}}$ will cause haemoglobin to release more ${\text{O}}_{\text{2}}$ to the tissues or to absorb more ${\text{O}}_{\text{2}}$ has to be identified.

Concept Introduction:

Haemoglobin:

• Composed of four polypeptide chain with a quaternary structure.
• A central heme molecule is there in each protein chain and each of the four hemes can bind with one ${\text{O}}_{\text{2}}$ molecule.
• Each heme molecule in its centre has ${\text{Fe}}^{\text{+2}}$
• The bright red haemoglobin with four oxygens is called oxy haemoglobin.
• The dark red-purple haemoglobin in which one or more oxygen is lost is called deoxyhaemoglobin.

The degree of saturation of haemoglobin is the percentage of heme units bound to oxygen at a given moment.

The binding of $O_2$ to haemoglobin depends on the $p{O}_2$ (partial pressure of oxygen) in the blood and the bonding strength, or affinity between oxygen and haemoglobin. Oxygen diffuses out of the arterial ends of tissue capillaries and carbon dioxide out of the tissue because of difference in partial pressure.

The factors which depend on the release of $O_2$ to the tissues and absorption of oxygens are temperature, ${\text{H}}^{\text{+}}$ concentration and ${\text{CO}}_{\text{2}}$ concentration.