Separation of H-Activity from Isolated Glycoproteins of Human O Erythrocyte Membranes
- 1 May 1974
- journal article
- Published by Wiley in Vox Sanguinis
- Vol. 26 (5) , 405-414
- https://doi.org/10.1111/j.1423-0410.1974.tb02715.x
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Membrane Structure: Some General PrinciplesScience, 1973
- A cross-linking study of the beef erythrocyte membrane: Extensive interaction of all the proteins of the membrane except for the glycoproteinsBiochemical and Biophysical Research Communications, 1973
- Cellular blood group substances. III. Isolation and characterization of glycosphingolipids with blood group H specificity from membranes of human erythrocytesBiochemistry, 1973
- Solubilization of human erythrocyte membrane glycoproteins and separation of the MN glycoprotein from a glycoprotein with I, S, and A activityBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Cross-linking the major proteins of the isolated erythrocyte membraneJournal of Molecular Biology, 1972
- Glycoproteins: Isolation from Cell Membranes with Lithium DiiodosalicylateScience, 1971
- Localization of A Antigen Sites on Human Erythrocyte GhostsNature, 1971
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- An apparent identity of 5-S RNA from free and membrane-bound reticulocyte ribosomesBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970
- Cellular blood-group substances. I. Isolation and chemical composition of blood-group ABH and Leb isoantigens of sphingoglycolipid natureBiochemistry, 1968