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CHAPTER 28

Hemoglobin

The easyavailability of blood hasresultedin many studies However, the differencesin tertiary structureamong them
of its constituents.Probably the most extensivelystudied are critical to the functional properties of each subunit.
componentis hemoglobin,the predominantprotein in the Each globin subunit has associated withit, by noncova-
red blood cell and the molecule responsiblefor transport- lent interaction, an Fe2+-porphyrincomplex known as a
ing oxygen,carbondioxide, andprotonsbetweenthe lungs hemegroup. Oxygenbinding occursat the hemeiron. The
and tissues.The study of hemoglobinhas led to a detailed predominant hemoglobin in adult erythrocytes is oe2f12,
knowledgeof how oxygen and carbon dioxidetransportis known as hemoglobinA1 (HbA). The structural and func-
accomplishedand regulatedand has provided insight into tional characteristicsof hemoglobinhavebeenworked out
the functioning of other allosteric proteins (Chapter 7). almost entirely through studies of HbA and its naturally
Hemoglobinis the first allosteric protein for which molec- occurring variants.
ular details of allosteric effector binding and the mecha- Each tetramerhas a molecular weight of about 64,500,
nism of allosteric action are known. Studies of the genes and each oe-like and fl-like chain has a molecular weight
coding for the globin polypeptide chains have provided of about 15,750 and 16,500, respectively. The subunits
a better understandingof many anemiasand of the regu- are situated at the corners of a tetrahedron(Figure 28-1).
lation of expressionof other eukaryotic genes. Correc- The structurechangesslightly during the binding and re-
tion of the genetic defects in sickle cell anemia and tha- leaseof oxygen. In a tetramer,dissimilar chains are more
lassemiaby the introduction of new genetic information stronglyjoined than similar chains.In dilute solution, oxy-
into bone marrow cells (gene therapy) is being actively hemoglobin dissociatesas follows:
explored.

28.1 Structure of Hemoglobins

Globin Chains
Mammalian hemoglobins are tetramersmade up of two
oe-like subunits (usually or) and two non-oesubunits (usu- There is no evidencefor the formation of |174or |174
ally 13, V, or 8). These subunits differ in primary struc- although in the absenceof ol-chains ~4 (HbH) forms.
ture but have similar secondaryand tertiary structures. Association involves salt bridges, hydrogen bonds, van

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