Self-digestion of human erythrocyte membranes. Role of adenosine triphosphate and glutathione
- 15 May 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 164 (2), 469-472
- https://doi.org/10.1042/bj1640469
Abstract
Intact human erythrocytes incubated at 37 degrees C, pH7.4, release a sialoglycopeptide similar in its chemical composition, immunological and aggregation properties to the glycopeptide released by isolated ‘ghost’ membranes. The presence of ATP or reduced glutathione at physiological concentrations in the incubation medium of ‘ghost’ membranes inhibits this self-digestion process.This publication has 17 references indexed in Scilit:
- Identification of a sialoglycopeptide released by self-digestion from human erythrocyte membranesBiochemical Journal, 1976
- Role of sialic acid in erythrocyte survival.1975
- Modifications of N-Acetylneuraminic Acid and Their Influence on the Antigen Activity of Erythrocyte GlycoproteinsEuropean Journal of Biochemistry, 1972
- Glycoproteins: Isolation from Cell Membranes with Lithium DiiodosalicylateScience, 1971
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- THE LOCALIZATION OF Mg-Na-K-ACTIVATED ADENOSINE TRIPHOSPHATASE ON RED CELL GHOST MEMBRANESThe Journal of cell biology, 1967
- The Contribution of Sialic Acid to the Surface Charge of the ErythrocyteJournal of Biological Chemistry, 1962
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- CHROMATOGRAPHY OF AMINO ACIDS ON SULFONATED POLYSTYRENE RESINSJournal of Biological Chemistry, 1951
- Microdetermination of plasma phospholipids by trichloroacetic acid precipitation.1950