Commonly abbreviated as Hb, Hemoglobin, or Heamoglobin, is the iron
containing oxygen in our red blood cells which transport
metalloproteins. All mammals on earth have hemoglobin, as it is a
necessary function in the blood. It contains globin, apoprotien, and
four heme groups (organic molecules with one atom of iron attached to
each).The gene for the hemoglobin protien can sometimes mutate. This
occurence results in one or more of many diseases, but most commonly
turns into Thalassemia or Sickle-cell disease.
Heme groups are located in each sub-unit of a hemoglobin molecule. A
heme group consists of a single iron atom, held in a heterocyclic ring,
commonly known as a "porphyrin". Oxygen binding takes place in this
iron atom. The one iron atom binds itself equally to all four nitrogens
in the center of the heterocyclic ring, which lies on one plane. In
addition, two bonds perpendicular to the plane on each side, are
sometimes formed with the iron to produce the fifth and sixth positions.
The name hemoglobin comes from "heme" and "globin". Globin is a generic
term used for a globular protein. Since any single subunit of
hemoglobin is made of a heme imbedded in a globular protein, the name
makes perfect sense. There are many heme containing hemoglobins and
proteins. Hemoglobin A is the most commonly known.
In adults, the most common hemoglobin is a tetramer (hemoglobin
containing 4 subunit proteins) called hemoglobin A. The subunits are
similar in structure, and approximatly the same size. Each subunits
molecular weight is about 16,000 daltons, for a total combined
molecular weight in the tetramer of approximatly 64,000 daltons. A
single heme is contained in each subunit of hemoglobin, so that the
overall binding capacity of human adults hemoglobin for oxygen is four
oxygen molecules.
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Tyler Brooker is the owner and operator of The Hemoglobin Index - www.hemoglobinspot.com, which is the best site on the internet for all hemoglobin related information.