Primary Structure of the Cytochrome c from the Great Grey Kangaroo, Macropus canguru

From the ¹ From the Biochemical Research Department, Abbott Laboratories, North Chicago, Illinois 60064

The complete amino acid sequence of the cytochrome c from heart tissue of the great grey kangaroo, Macropus canguru, has been established from the structures of the chymotryptic peptides and the amino acid compositions and partial sequences of the tryptic peptides. This primary structure bears all of the characteristics of the cytochromes c of the "mammalian type," showing the typical clustered distribution of hydrophobic and basic residues, a single polypeptide chain 104 residues long, and, like other cytochromes c from vertebrate species, an acetylated amino-terminal residue. Position 33 is occupied by an asparaginyl residue as contrasted to the histidine occurring at this location in all but one of the other cytochromes c of known amino acid sequence. Kangaroo heart cytochrome c differs from the horse, human, pig, cow, chicken, tuna, moth, and bakers' yeast proteins by 7, 10, 6, 6, 12, 20, 29, and 45 residues, respectively.

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