title: Changes in proteolytic susceptibility of human erythrocyte membrane proteins during red blood cell aging.
abstract: The method employed facilitated analysis of the digestion of denatured proteins, depleted in their natural membrane environment. The susceptibility of human erythrocyte membrane proteins to digestion with trypsin was studied by the two-dimensional electrophoretic method. Ghosts were isolated from erythrocytes fractionated according to density (age). Spectrin and band 3 protein from membranes isolated from the youngest cells were significantly more slowly degraded than proteins from middle-age cell membranes and from the oldest cells.
authors.affiliation: Department of Biophysics, University of Lódź, Poland.
authors.forename: M
authors.initials: M
authors.lastname: Gaczyńska
mesh_terms: D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D004905:Erythrocyte Aging / Q000502:physiology*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000097:blood*; D011489:Protein Denaturation / Q000502:physiology; D013049:Spectrin / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism*
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D008565:Membrane Proteins; D013049:Spectrin; D014357:Trypsin