Isolation of Cyanogen Bromide Cleavage Peptides from Myoglobins

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Abstract
The chemical cleavage of apomyoglobins by the cyanogen bromide procedure1 has provided frag­ ments suitable for sequence analysis2, 3 and for studies of physical 4-6 and immunochemical pro­ perties 7. Offord 8 has used a peptide obtained from the cyanogen bromide cleavage of ribonuclease in studies aimed at the semi-synthesis of a protein. The purpose of this report is to present conditions that reliably separate pure peptide fragments produced from the apomyoglobins of several species. A single gel filtration step obviates the need for additional purification2,3,6. The evidence re­ ported here concerns specifically the apoprotein of sperm whale (Physeter catodon) and California sea lion (Zalophus californianus) . The procedure additionally has heen applied9 without modification to the separation of the cyanogen bromide fragments of apomyoglobin from Amazon River dolphin (lnia geoffrensis), Minke whale (Balaenoptera aeutoro- strala), gray whale (Eschrichtius gibbosus), Dali porpoise (Phocoenoides dalli dalli) and the bottlenosed dolphin (Tursiops truncatus). Cyanogen bromide fragments from two of the variant myoglo­bins which occur to a minor extent in the sperm whale were also separated by this method 10.

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