Abstract
A single form of cytochrome b5 has been isolated in highly purified form from the cytosolic fraction of rabbit erythrocytes by sequential chromatography on DE-52 cellulose, Sephadex G-75, and DEAE-Sephadex A50. The cytochrome is structurally similar to the N-terminal, heme-binding domain of rabbit liver microsomal cytochrome b5. Like the liver protein, it is blocked at the amino terminus. Its amino acid composition is similar to that of residues 1-97 of the microsomal protein. With one exception, tryptic peptides derived from apo-cytochrome b5 of rabbit erythrocytes co-elute with the tryptic peptides obtained from a soluble hemepeptide fragment of microsomal cytochrome b5. These findings, together with amino acid sequence analysis of the carboxyl terminal tryptic peptides, identify the erythrocyte cytochrome b5 as a 97-residue peptide.
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