Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase

J Biol Chem. 1982 Feb 10;257(3):1438-42.


Band 3, the anion transport protein of the human erythrocyte, provides the site of association of certain glycolytic enzymes with the membrane. We have now demonstrated that glyceraldehyde-3-P dehydrogenase is inhibited, reversibly and completely, when membrane bound. The inhibition was competitive with respect to NAD+ and arsenate, but was noncompetitive with glyceraldehyde-3-P. Peptide fragments containing the NH2-terminal 23 residues of band 3 also inhibited the enzyme and displaced it from ghosts. Thus, the red cell membrane binding site for glyceraldehyde-3-P dehydrogenase is the same as that for aldolase, the polyanionic NH2-terminal region of the band 3 polypeptide.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Anion Exchange Protein 1, Erythrocyte
  • Anions
  • Blood Proteins / metabolism*
  • Erythrocyte Membrane / metabolism*
  • Erythrocytes / metabolism*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / blood*
  • Humans
  • Kinetics
  • Osmolar Concentration
  • Protein Binding


  • Anion Exchange Protein 1, Erythrocyte
  • Anions
  • Blood Proteins
  • Glyceraldehyde-3-Phosphate Dehydrogenases