Oxidation of methionine causes a change in the electrophoretic mobility of the major sialoglycoprotein of the human erythrocyte membrane
- 30 September 1977
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 494 (2) , 441-445
- https://doi.org/10.1016/0005-2795(77)90178-7
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- The effect of carboxymethylating a single methionine residue on the subunit interactions of glycophorin ABiochemistry, 1976
- Subunit structure of human erythrocyte glycophorin ABiochemistry, 1976
- Selective oxidation of methionine residues in proteinsBiochemistry, 1975
- Fractionation of the major sialoglycopeptides of the human red blood cell membraneBiochemical and Biophysical Research Communications, 1975
- Human erythrocyte membrane sialoglycoproteins: A study of interconversionBiochemical and Biophysical Research Communications, 1974
- Subunit structure of the major human erythrocyte glycoprotein: Depolymerization by heating ghosts with sodium dodecyl sulfateBiochemical and Biophysical Research Communications, 1973
- Separation and some properties of the major proteins of the human erythrocyte membraneBiochemical Journal, 1972
- [31] Oxidation with hydrogen peroxidePublished by Elsevier ,1972
- Glycoproteins: Isolation from Cell Membranes with Lithium DiiodosalicylateScience, 1971
- Starch-gel electrophoresis—Application to the classification of pituitary proteins and polypeptidesMetabolism, 1964