N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts

Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next.