Biomaterial Database

Binding of 2,3-diphosphoglycerate by spectrin and its effect on oxygen affinity of hemoglobin. 1978

N Shaklai, and L Benitez, and H M Ranney

The relationships between spectrin, a structural protein of the red blood cell (RBC) membrane facing the cytoplasm, and hemoglobin were studied. The oxygen-binding properties of stripped hemoglobin were not altered by the presence of spectrin, but the interaction of hemoglobin with organic phosphates was reduced by the addition of spectrin. The presence of the enzyme glyceraldehyde 3-phosphate dehydrogenase (G3PD), another component of the RBC membrane used as a control, did not change the oxygen affinity of either stripped hemoglobin or of hemoglobin solutions containing phosphates. Binding studies using the gel filtration method at pH 7.3 indicated reversible binding of 2,3-diphosphoglycerate to spectrin. A unit of 220,000 daltons was calculated to have seven binding sites and a binding constant of 1.2 X 10(4) M-1. A mechanism is proposed in which spectrin may facilitate oxygen transport for hemoglobin molecules reaching the membrane.

UI	MeSH Term	Description	Entries
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D010100	Oxygen	An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.	Dioxygen,Oxygen-16,Oxygen 16
D004163	Diphosphoglyceric Acids	Glyceric acids where two of the hydroxyl groups have been replaced by phosphates.	Bisphosphoglycerates,Acids, Diphosphoglyceric
D004910	Erythrocyte Membrane	The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.	Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D006454	Hemoglobins	The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.	Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001667	Binding, Competitive	The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.	Competitive Binding
D013049	Spectrin	A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.	alpha-Spectrin,beta-Spectrin,alpha Spectrin,beta Spectrin