Proteomic analysis of RBC membrane protein degradation during blood storage.

摘要: Two-dimensional gel electrophoresis and mass spectrometry were used to identify protein profile changes in red blood cell membranes stored over time under atmospheric oxygen, the presence or absence of protease inhibitors. New spots with lower molecular masses, ranging between 7 15 kDa observed during first days storage, while time, further fragments high-molecular-mass aggregates appeared, seen as a smearing upper part gel. Some turned out be shifts isoelectric point, consequence chemical oxidations. All these new generated result attack by reactive oxygen species (ROS). Protein identification revealed that most modified proteins are located cytoskeleton. During oxidative degradation was prevalently band 4.2, minor extent bands 4.1 3, spectrin. After 14 days, there from β-actin, glyceraldehyde-3-phosphate dehy...