Abstract
The C-terminal cyanogen bromide fragment of myoglobin from bottle nosed dolphin was digested with trypsin and two different derivatives of the digest were prepared, one being deuteroacetylated and deuteropermethylated, the other being submitted to one step of Edman degradation and then acetylated and permethylated. Comparison of the results obtained by computerized interpretation of the mass spectra of these two derivatives, combined with previous information about the sample, facilitated the sequence determination of all the peptides in the sample. Alignment of the peptides could then be carried out by homology with myoglobin from other cetaceans.