hemoglobin I

he·mo·glo·bin I

[MIM*141800.0055]
an abnormal Hb with a single α chain substitution, molecular formula α216Lys→Gluβ2A; a thalassemialike syndrome has been found in people heterozygous for both Hb I and α-thalassemia genes, with formation of about 70% Hb I.
References in periodicals archive ?
What all of the methods have in common is that they do not require a blood sample to determine an individual's hemoglobin; instead, hemoglobin is measured by means of a spectrophotometric sensor.
Normal adult hemoglobin is Hemoglobin A, consisting of two alpha chains and two beta chains.
This relationship between the partial pressure of oxygen and the oxygen saturation of hemoglobin is described in the oxygen-dissociation curve.
Hemoglobin is the iron-containing oxygen-transport metalloprotein in the red blood cells1.
The oxygen binding affinity of natural human hemoglobin is too high when it is free in the blood stream (not contained within erythrocytes) because of a lack of allosteric control.
Hemoglobin is the protein responsible for absorbing oxygen when the red blood cell passes through the lungs.
Hemoglobin is a protein-iron compound that carries oxygen and is located in red blood cells.
Hemoglobin is "a little shuttle system," explains Somatogen scientist Bill Freitag.
As it turns out, polymerized hemoglobin is too big to slip through blood vessels and take up nitric oxide, so it's less prone to raise blood pressure than lone hemoglobin molecules are, Olson says.