title: Neutral serine proteinase and metalloproteinase strongly bound to human erythrocyte membrane.
abstract: Human and bovine erythrocyte ghosts contain a proteolytic system strongly related to membranes. Two proteinases were isolated from human erythrocyte ghosts depleted in most peripheral proteins by extraction with Triton X-100, chromatography on DEAE-cellulose and preparative electrophoresis (SDS-PAGE). The enzymes which were strongly bound to membrane serine proteinase (relative molecular weight 23 kD) and metalloproteinase (28 kD), are probably the integral membrane proteins.
authors.affiliation: Department of Biophysics, University of Lódź, Poland.
authors.forename: M
authors.initials: M
authors.lastname: Gaczyńska
authors.forename: G
authors.initials: G
authors.lastname: Bartosz
mesh_terms: D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000737:chemistry / Q000201:enzymology*; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis; D008666:Metalloendopeptidases / Q000032:analysis*; D008970:Molecular Weight; D017830:Octoxynol; D011092:Polyethylene Glycols; D012697:Serine Endopeptidases / Q000032:analysis*
chemical_list: D008565:Membrane Proteins; D011092:Polyethylene Glycols; D017830:Octoxynol; D012697:Serine Endopeptidases; D008666:Metalloendopeptidases