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Fast atom bombardment mass spectrometric investigation of in vitro degradation within the disulfide‐linked core of atrial natriuretic factor
Author(s) -
Chen TengMan,
Ackermann Bradley L.,
Coutant John E.,
Berman Judd M.,
Pelton John T.
Publication year - 1989
Publication title -
biomedical and environmental mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0887-6134
DOI - 10.1002/bms.1200180104
Subject(s) - chemistry , thermolysin , hydrolysis , fast atom bombardment , endopeptidase , peptide , neprilysin , in vitro , degradation (telecommunications) , peptide bond , mass spectrometry , trypsin , chromatography , biochemistry , enzyme , telecommunications , computer science
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 5–23 ‐NH 2 and rANF 7–23 ‐NH 2 were digested with the endopeptidase thermolysin. These truncated analogs were selected to investigate metabolism within the disulfide‐linked core of ANF, particularly at the Cys 7 Phe 8 bond. While this position was the site of initial hydrolysis for rANF 5–23 ‐NH 2 ( t 1/2 = 0.5 min), the Cys 7 Phe 8 bond remained intact for all observed degradation products of rANF 7–23 ‐NH 2 ( t 1/2 = 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.