ISSN:
0887-6134
Keywords:
Chemistry
;
Analytical Chemistry and Spectroscopy
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
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, rANF5-23-NH2 and rANF7-23-NH2 were digested with the endopeptidase thermolysin. These truncated analogs were selected to investigate metabolism within the disulfide-linked core of ANF, particularly at the Cys7—Phe8 bond. While this position was the site of initial hydrolysis for rANF5-23-NH2 (t1/2 = 0.5 min), the Cys7—Phe8 bond remained intact for all observed degradation products of rANF7-23-NH2 (t1/2 = 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.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bms.1200180104
