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Mass spectrometric characterization of bovine chromaffin granule peptides related to chromogranin B.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 1992 Mar 27; Vol. 1120 (1), pp. 105-12. - Publication Year :
- 1992
-
Abstract
- 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.
- Subjects :
- Amino Acid Sequence
Animals
Cattle
Chromogranin B
Chromogranins isolation & purification
Mass Spectrometry
Molecular Sequence Data
Peptide Fragments chemistry
Pyrrolidonecarboxylic Acid analogs & derivatives
Trypsin
Chromaffin Granules chemistry
Chromogranins chemistry
Neuropeptides chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1120
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 1554736
- Full Text :
- https://doi.org/10.1016/0167-4838(92)90430-l