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Found Hemoglobin 12 times.

Displaying results 1 to 10.

1. Hemoglobin
The protein in red blood cell s that carries oxygen; it contains heme as a prosthetic group and is composed of four polypeptide s. The types of these polypeptide chains are called alpha, beta, gamma, and delta.

2. Hemoglobin A (haemoglobin A)
Hemoglobin A is the normal form of the protein hemoglobin which is found in adults. It is composed of two alpha chains and two beta chains.

3. Hemoglobin A1C (HbA1C)
The substance of red blood cell s that carries oxygen to the cells and sometimes joins with glucose . Because the glucose stays attached for the life of the cell (about 4 months), a test to measure hemoglobin A1C shows what the person's average blood glucose level was for that period of time.

4. Hemoglobin C (haemoglobin C)
Hemoglobin C is an abnormal version of the protein hemoglobin . The sixth amino acid of the normal beta chain, glutamic acid , is replaced by lysine in hemoglobin C. This mutation causes the red blood cell to be less flexible.

5. Hemoglobin E (haemoglobin E)
Hemoglobin E is an abnormal version of the protein hemoglobin , found in Southeast Asia, which plays a role in such medical conditions as microcythemia, target cell formation, and mild hemolytic anemia. The beta chain of the hemoglobin is altered because of a mutation .

6. Hemoglobin electrophoresis (haemoglobin electrophoresis)
Hemoglobin electrophoresis is a lab technique, a type of electrophoresis , used to separate hemoglobin protein s from each other with an electric current.

7. Hemoglobin F (haemoglobin F)
Hemoglobin F is the normal form of the protein hemoglobin which is found in the fetus .

8. Hemoglobin H (haemoglobin H)
Hemoglobin H is an abnormal version of the protein hemoglobin . The normal hemoglobin is composed of two alpha and two beta polypeptide chains; hemoglobin H is composed of four beta chains. The molecule has a very high affinity to oxygen, but is very inefficient at transporting it.

9. Hemoglobin S (haemoglobin S)
Hemoglobin S is an abnormal version of the protein hemoglobin . The sixth amino acid of the normal beta chain, glutamic acid , is replaced by valine with gluconic acid . This mutation causes the red blood cell to take on a sickle shape, and is the cause of the sickle cell trait condition (when the individual is heterozygous for this mutant hemoglobin) and the disease of sickle cell anemia (when the individual is homozygous for this mutant hemoglobin).

10. Hemoglobin
A red pigment in red blood cells that can bind with oxygen and is largely responsible for the blood's oxygen-carrying capacity. Hemoglobin is composed of four polypeptide chains, two alpha (a) and two beta (b) chains.


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