Erythrocytes glyceraldehyde-3-phosphate dehydrogenase

From an operational viewpoint, there is a spectrum of proteins associated with membranes. At one end of the spectrum are those proteins such as erythrocyte glyceraldehyde-3-phosphate dehydrogenase (G-3-PD) that appear to be bound to the membrane through coulombic forces and which are released under conditions utilizing changes in ionic strength. Beyond this, one encounters the vast majority of membrane-bound proteins which interact with both the hydrophilic and hydrophobic domains of the membrane, while at the other end of the spectrum lie those proteins located entirely within the hydrocarbon core of the membrane. This wide spectrum dictates careful selection... 

One of the major integral proteins of the erythrocyte membrane is the anion channel, or band-3 protein, which moves Cl- and HC03 anions across the membrane. The anion transporter has two identical subunits with molecular weights of about 95,000, and each subunit probably has 10 or 11 transmembrane helices. The band-3 protein is attached to the spectrin cytoskeleton through a smaller protein, anky-rin. The cytosolic domain of the anion transporter also binds the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. 

Kots, A. Y., Skurai, A. V., Sergienko, E. A., Bulargina, T. V., and Sevorin, B. S. (1992). Nitroprusside stimulates the cysteine-specific mono(ADP-ribosylation) of glyceraldehyde-3-phosphate dehydrogenase fi"om human erythrocytes. FEES Lett. 300, 9-12. 

May, J. (1986). Photoaffinity Labeling of Glyceraldehyde-3-phosphate Dehydrogenase by an Aryl Azide Derivative of Glucosamine in Human Erythrocytes, J. Biol. Chem. 261 2542-2547. 

Shin, B. C., and Carraway, K. L., 1973, Association of glyceraldehyde 3-phosphate dehydrogenase with the human erythrocyte membrane, /. Biol. Chem. 248 1436. 

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