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A comparative study of spectrin: A protein isolated from red blood cell membranes

1970; Elsevier BV; Volume: 200; Issue: 1 Linguagem: Inglês

10.1016/0005-2795(70)90050-4

1878-1454

Thomas W. Tillack, Sally L. Marchesi, V. Marchesi, Edward Steers,

Protein Structure and Dynamics

1. A membrane-bound protein, called spectrin, has been solubilized from human, guinea pig, horse, sheep, and rabbit erythrocyte ghosts by dialysis against EDTA and β-mercaptoethanol. 2. Spectrin accounted for approx. 20% of the total membrane protein in all these species and was free of carbohydrate and lipid. 3. Spectrin preparations from each species were homogeneous when studied by gel filtration, polyacrylamide gel electrophoresis, and immunoprecipitin reactions. 4. Spectrin appeared to be a very similar, possibly homologous, protein in the red cell membranes of different species. The amino acid compositions and electrophoretic patterns were nearly identical. Antiserum to guinea pig and human spectrin cross-reacted with all the other species. 5. Comparison by disc gel electrophoresis of peptides produced by CNBr cleavage of human, horse, and sheep spectrin showed similar numbers of peptides but different electrophoretic migrations, indicating some differences in amino acid sequence in the different molecules.