Biochemistry: Haemoglobin

Martini, Frederic, Judi L. Nath, and Edwin F. Bartholomew.Fundamentals of Anatomy & Physiology. 9th ed. San Francisco, CA: Benjamin Cummings, 2012. Print.

Iron Deficiency Anemia affects millions of individuals across the world. This disease strikes many more women than men and has harmful effects on all who suffer from this deficiency that causes oxygen-carrying capacity to decrease. The causes can vary amongst different groups, but the aggravating symptoms remain constant. Much of the research on Iron Deficiency Anemia concentrates on not only the treatment of this disease, but also the prevention of it. To attain a better understanding of how to treat this problem, one must clearly know what Iron Deficiency Anemia means, what causes this disease, the effects of it, and finally how to cure it.

“Erythrocytes contain haemoglobin, an important respiratory pigment that is essential for human life” (Strech, Beryl; Whitehouse, Mary;, 2010) Haemoglobin is very important because it is an iron-containing protein.

Iron is one of the important minerals that is required for our bodies to function properly. Most of the iron in our body is found in the blood such as haemoglobin, approximately 60 -70% of the human body’s iron is found in the haemoglobin, a protein in the blood that transports oxygen. Iron is also present in muscle tissue and some enzymes. There are two types of iron in the body which are “Heme Iron” from animal products and “Non-Heme Iron” vegetables and

J.) As Cari’s Pco2 and alkaline blood pH rose, how was the oxygen-carrying capacity of hemoglobin affected?

BIOL 203: Human Anatomy and Physiology Midterm Review 10-15-2015 LAB MIDTERM Tuesday, October 20th, 2015 at 8:00-9:30PM in Elliott Hall of Music BRING YOUR PURDUE ID!!!!!! EVENING EXAM TAKES THE PLACE OF YOUR REGULARLY SCHEDULED LAB FOR THE WEEK OF OCT. 12!

Marieb, Elaine N. Essentials of Human Anatomy and Physiology,VitalSource eBook for DeVry University. Pearson Learning Solutions, 02/2012. VitalBook file.

The blood protein in Methemoglobinemia are unable to carry oxygen, which makes it harder for the tissue to get the amount of oxygen

Methemoglobinemia can be either acquired or congenital. When methemoglobinemia is acquired the mechanism that reduces methemoglobin is not able to keep up with the amount of oxidation that is occurring due to the various methods of acquiring methemoglobinemia [2]. There are two primary reasons for congenital methemoglobinemia; either there is a presence of an abnormal structure of the hemoglobin molecule, called hemoglobin M, or a deficiency in the enzymes cytochrome b5 methemoglobin reductase or glucose-6-phosphate dehydrogenase (G6PD) [5]. There are two main types of congenital methemoglobinemia, type I and type II. Type I methemoglobinemia is where the enzyme deficiency only affects the erythrocytes, and is easily

cell affects the beta-goblin subunit and is given the name HBB gene. This gene mutation causes in a change in the beta-goblin structure by replacing glutamic acid with valine in the sixth position in the polypeptide chain. This gene is found on chromosome 11. This change results in an abnormal version of the beta-goblin which is called haemoglobin S (HbS).

Platelets and leukocytes are less than 0.1% of formed elements but nearly 99.9% are nuclei-lacking red blood cells, whose biconcave disk-shape increases surface area and allows for the diffusion of oxygen (Martini et al., 2015). Erythrocytes contain hemoglobin proteins, where each protein has four iron-containing heme groups that can bind one oxygen molecule each (Surgenor, 2013). In other words, each hemoglobin protein can carry four oxygen molecules and there are over 250 million hemoglobin proteins per cell.

The binding of oxygen to hemoglobin is cooperative. This means that once an oxygen molecule is bound to an iron of one of the four heme groups of deoxygenated hemoglobin, the affinity of the resulting oxygenated hemoglobin molecule towards oxygen will be greater than that of the starting deoxygenated hemoglobin. As a result, the binding of a second oxygen molecule

Investigating haemoglobin (Hb) concentration in blood samples using the haemoglobincyanide method and in foetal haemoglobin samples

These cells' cytoplasm is rich in hemoglobin, an iron-containing biomolecule that can bind oxygen and is responsible for the blood's red color.

Haemoglobin is located in the red blood cell and its primary function is to transport oxygen from the lungs to the body’s cells and tissues. Haemoglobin needs to readily collect as much oxygen