Abstract
AbstractThis report describes the formation of a non‐covalent complex between two tryptic peptides of horse heart cytochrome‐c. All amino functions of cytochrome‐c were completely protected with the methylsulfonylethyloxycarbonyl (Msc) group. Trypsin split the protected product specifically at Arg38. After separation the fragments were deprotected by a very short treatment with a base.The complex resulting from the deprotected peptides, exhibited a completely developed 695 nm band, and an enhanced oxidase but diminished reductase activity in comparison with native horse heart cytochrome‐c.
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