HEMOGLOBIN

1. Types of HB

1.1. The most common ones are:  HbA, HbA2, HbE, HbF, HbS, HbC, HbH, and HbM. Healthy adults only have significant levels of only HbA and HbA2

2. Rate of HB

2.1. The healthy range for hemoglobin is: For men, 13.2 to 16.6 g per dl. For women, 11.6 to 15 g per dl.

3. High and low HB

3.1. Low hemoglobin that's caused by low iron levels is known as iron deficiency anemia.

3.2. high hemoglobin count is associated with high hemoglobin levels, which means that your hemoglobin has an increased oxygen-carrying capacity than normal.

4. Role of Haemoglobin

4.1. to transport oxygen

4.2. needs to readily associate with oxygen at the surface where gas exchange occurs.

4.3. readily dissociate oxygen at those tissues requiring it

4.4. Haemogobin changes shape to take up and release oxygen in the presence of certain substances .

5. Structure of haemoglibin

5.1. Primary structure Consists of four polypeptide chains.

5.2. Secondary structure Each of these chains is coiled into a helix

5.3. Tertiary structure In which each polpeptide chain is folded into a precise shape-very important to be able to carry oxygen

5.4. Quaternary structure All four polypedtide chains are linked together to form a spherical molecule. Each chain is associated with a haem group. Each Fe+ ion combines with one oxygen molecule

6. Definition

6.1. a protein in your red blood cells that carries oxygen to your body's organs and tissues and transports carbon dioxide from your organs and tissues back to your lungs