Effects of chemical modification of membrane thiol groups on hemolysis of human erythrocytes under hydrostatic pressure

Biochim Biophys Acta. 1994 Nov 2;1195(2):205-10. doi: 10.1016/0005-2736(94)90257-7.


Membrane stability of the human erythrocyte under high pressure was examined by modifying membrane SH-groups with NEM or diamide. Hemolysis at 200 MPa of chemically modified erythrocytes was significantly suppressed by the prolonged incubation of them in a reagent-free medium above 30 degrees C prior to the application of high pressure. However, there was no detectable change regarding membrane phospholipid distribution, CD spectra and SDS-PAGE of membrane proteins, and intracellular K+ concentration during the incubation. On the other hand, the data of protein-spin labeling and SH-group content showed that the SH-groups buried in membrane proteins appeared on their surface by conformational changes of membrane proteins induced during the incubation. The extraction of peripheral proteins from NEM-treated membranes in 0.1 N NaOH was considerably suppressed by the incubation. These results suggest that, upon chemical modification of membrane SH-groups, protein-protein interactions are modulated during prolonged incubation above 30 degrees C so that high pressure-induced hemolysis is suppressed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Diamide / pharmacology
  • Erythrocyte Membrane / chemistry*
  • Ethylmaleimide / pharmacology
  • Hemolysis*
  • Humans
  • Hydrostatic Pressure
  • Membrane Lipids / analysis
  • Membrane Proteins / chemistry
  • Phospholipids / analysis
  • Protein Conformation
  • Sulfhydryl Compounds / physiology*


  • Membrane Lipids
  • Membrane Proteins
  • Phospholipids
  • Sulfhydryl Compounds
  • Diamide
  • Ethylmaleimide