Ionic-strength-dependent changes in the structure of the major protein of the human erythrocyte membrane.
The effect of ionic strength on the proteolysis by trypsin of the major membrane-penetrating protein (polypeptide 3) in the erythrocyte membrane was studied. Both the intracellular and extracellular regions of the protein are susceptible to trypsin proteolysis under hypo-osmotic conditions, whereas under iso-osmotic conditions the extracellular region of the protein is resistant to trypsin, and the intracellular region yields only two cleavage products with trypsin. Studies of the fragments obtained from polypeptide 3 by trypsin digestion under iso-osmotic conditions of 'ghosts' radioiodinated with lactoperoxidase confirmed our earlier conclusions that the polypeptide chain of polypeptide 3 traverses the membrane twice. Ionic-strength-dependent changes were also observed in the incorporation of iodine by lactoperoxidase into the individual extracellular tyrosine sites of the protein. These results show that polypeptide 3 undergoes ionic-strength-dependent changes in structure.
D001345:Autoradiography; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D007457:Iodine Radioisotopes; D007784:Lactoperoxidase; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism*; D009994:Osmolar Concentration; D013820:Thermolysin / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology; D014443:Tyrosine / Q000032:analysis
D007457:Iodine Radioisotopes; D008565:Membrane Proteins; D014443:Tyrosine; D007784:Lactoperoxidase; D014357:Trypsin; D013820:Thermolysin