Fast atom bombardment mass spectrometric investigation of in vitro degradation within the disulfide-linked core of atrial natriuretic factor
✍ Scribed by Teng-Man Chen; Bradley L. Ackermann; John E. Coutant; Judd M. Berman; John T. Pelton
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 662 KB
- Volume
- 18
- Category
- Article
- ISSN
- 1076-5174
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✦ Synopsis
The use of high-performance liquid chromatography and fast atom bombardment mass spectrometry are shown to be an efficient combination for investigating protease-mediated digestion of synthetic analogs of the peptide hormone ANF (atrial natriuretic factor). As examples of the reported methodology, rANF,-,,-NH, and rANF,-,,-NH, were digested with the endopeptidase thermolysin. These truncated analogs were selected to investigate metabolism within the disulfidelinked core of ANF, particularly at the Cys7-Phe8 bond. While this position was the site of initial hydrolysis for rANF,-,,-NH, (t,,, = 0.5 min), the Cys7-Phe8 bond remained intact for all observed degradation products of rANF,-,,-NH, (t,,, = 16 min). These findings suggest that improved stability towards endopeptidase-mediated core hydrolysis may be conferred to analogs of ANF by removal of the first six residues from the N-terminus.