k Haemoglobin molecule, illustration Illustration of a haemoglobin molecule HbAB. Haemoglobin is composed of four subunits, two alpha pink ribbon and two beta blue ribbon. HbAB is the main functional constituent of the red blood cell, serving as the oxygencarrying protein. In the centre, the bisphosphoglyceric acid BGP binding site is shown red and yellow spheres. When bound, BPG decreases the affinity for oxygen of HbAB. The figure also shows the haem groups of beta chains, in rod model, occupied by oxygen and carbon monoxide molecules. Stock Photo - Afloimages
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Haemoglobin molecule, illustration Illustration of a haemoglobin molecule  HbAB . Haemoglobin is composed of four subunits, two alpha  pink ribbon  and two beta  blue ribbon . HbAB is the main functional constituent of the red blood cell, serving as the oxygen carrying protein. In the centre, the bisphosphoglyceric acid  BGP  binding site is shown  red and yellow spheres . When bound, BPG decreases the affinity for oxygen of HbAB. The figure also shows the haem groups of beta chains, in rod model, occupied by oxygen and carbon monoxide molecules.
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Haemoglobin molecule, illustration

Illustration of a haemoglobin molecule (HbAB). Haemoglobin is composed of four subunits, two alpha (pink ribbon) and two beta (blue ribbon). HbAB is the main functional constituent of the red blood cell, serving as the oxygen-carrying protein. In the centre, the bisphosphoglyceric acid (BGP) binding site is shown (red and yellow spheres). When bound, BPG decreases the affinity for oxygen of HbAB. The figure also shows the haem groups of beta chains, in rod model, occupied by oxygen and carbon monoxide molecules.

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