Mass spectrometric characterization of bovine chromaffin granule peptides related to chromogranin B.
Peptides were extracted from the lysate of isolated bovine chromaffin granules. Following reversed-phase HPLC purification, the fractions were analyzed by FAB/MS. The presence of methionine-enkephalin and leucine-enkephalin was indicated by their chromatographic retention time and by the m/z value of their protonated molecules. As to five new peptides related to chromogranin B, prominent protonated molecules were observed at m/z 1746, 1446, 1333, 977 and 901. Trypsinolysis resulted in a common loss of a component with mass 545, pointing to a structural relationship and a common precursor molecule. The peptide showing a (M+H)+ ion at m/z 1746 could be identified as a novel, recently reported, neuropeptide derived from chromogranin B, whereas the other peptides with (M+H)+ ions at m/z 1446, 1333, 977 and 901 could be characterized as smaller fragments of this peptide. Peptidase-guided sequence analysis and MS/MS analysis provided sequence information.[1]References
- Mass spectrometric characterization of bovine chromaffin granule peptides related to chromogranin B. Dillen, L., Boel, S., De Potter, W.P., Claeys, M. Biochim. Biophys. Acta (1992) [Pubmed]
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