Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin
Open Access
- 1 April 1979
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 254 (7) , 2533-2541
- https://doi.org/10.1016/s0021-9258(17)30254-5
Abstract
No abstract availableThis publication has 33 references indexed in Scilit:
- Association of spectrin with its membrane attachment site restricts lateral mobility of human erythrocyte integral membrane proteinsJournal of Supramolecular Structure, 1978
- Human erythrocyte spectrin: Phosphorylation in intact cells and purification of the 32P-labeled protein in a non-aggregated stateLife Sciences, 1977
- Physico-chemical characterization of the spectrin tetramer from bovine erythrocyte membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1976
- Surface Modulation in Cell Recognition and Cell GrowthScience, 1976
- Transmembrane control of the receptors on normal and tumor cellsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1976
- Membrane proteins related to anion permeability of human red blood cellsThe Journal of Membrane Biology, 1974
- Protein a from Staphylococcus aureus. Its isolation by affinity chromatography and its use as an immunosorbent for isolation of immunoglobulinsFEBS Letters, 1972
- Modification and introduction of a specific radioactive label into the erythrocyte membrane sialoglycoproteinsBiochemical and Biophysical Research Communications, 1972
- Isolation and characterization of a water-soluble protein from bovine erythrocyte membranesBiochemical and Biophysical Research Communications, 1971
- THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONSAnnals of the New York Academy of Sciences, 1949