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The Restricted Tryptic Cleavage of Cytochrome b₅

From the ¹ From the Department of Biological Chemistry, Washington University School of Medicine, Saint Louis, Missouri 63110

Two major heme protein components have been identified in cytochrome b₅ preparations from calf liver by electrophoresis and have been separated chromatographically. These two forms of cytochrome b₅ differ in that one contains a carboxyl-terminal glutamylserine peptide sequence which is absent from the second. Tryptic digestion of either heme protein species yields the same core heme peptide by the cleavage of two peptides, one from the carboxyl-terminal and one from the amino-terminal end. The amino acid sequence of the small peptides released by trypsin and the peptide sequence in cytochrome b₅ was determined. The core heme peptide contains 81 amino acid residues and is indistinguishable in its spectral and catalytic properties from the original cytochrome b₅ preparations. This heme peptide thus provides the simplest unit for a complete analysis of the catalytic properties and the structure of cytochrome b₅.

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