Abstract
Tandem mass spectrometry with a four-sector type mass spectrometer was used to elucidate the structures of minor components of the peptidyl antibiotic P168s (leucinostatins). As N-terminal fragments, ions by B-type cleavage were dominant, while V-type cleavages were observed along with X, Y, and Z types as C-terminal ions. The V-type ions were predominant in the cleavages of the amino terminals of leucyl and hydroxyleucyl residues. The structures of several minor components could be deduced from the tandem mass spectra.
Original language | English |
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Pages (from-to) | 1079-1085 |
Number of pages | 7 |
Journal | Bioscience, biotechnology, and biochemistry |
Volume | 56 |
Issue number | 7 |
DOIs | |
Publication status | Published - 1992 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry