The isolation and functional identification of a protein from the human erythrocyte 'ghost'.
A protein, initially identified as a band on polyacrylamide-gel electrophoresis of erythrocyte ;ghosts', was isolated by selective extraction of ;ghosts' with EDTA solutions. The molecular weight of the polypeptide chain was estimated as 33000 and it represents approx. 5% of the membrane protein. The N-terminal sequence of the protein was established. Comparison with known protein sequences suggested that the protein might be the erythrocyte d-glyceraldehyde 3-phosphate dehydrogenase. This identification was confirmed by direct enzyme assay. It is suggested that this enzyme, which is strongly retained by erythrocyte ;ghosts' on haemolysis of erythrocytes, is unlikely to be an integral part of the structure of the erythrocyte membrane.
D000178:Acrylamides; D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000032:analysis*; D004492:Edetic Acid; D004586:Electrophoresis; D004912:Erythrocytes / Q000032:analysis* / Q000201:enzymology; D005782:Gels; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification; D006801:Humans; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification*
D000178:Acrylamides; D005782:Gels; D010455:Peptides; D011506:Proteins; D004492:Edetic Acid; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases