Peptide sequencing by partial acid hydrolysis and high resolution plasma desorption mass spectrometry.

ABSTRACT

A method of deriving peptide sequence information using partial acid hydrolysis in combination with accurate mass measurements and immonium ion analysis provided by high-resolution plasma desorption mass spectrometry has been developed. The technique is very simple in terms of the chemistry and involves a short-time (3-30 min) incubation of the peptide in 1N-6N HCl at 100-110 degrees C with subsequent mass spectrometric analysis. Partial acid hydrolysis is found to produce sequence-specific segments, often ladder-like, although not always a complete set. Two application examples of the method are given the linear peptide bradykinin and desmopressin, a peptide with an internal S-S bond and a non-amino-acid constituent. The technique has proved to be particularly useful in cases where some a priori information on the peptide structure was already known or where the automated Edman degradation technique might yield erratic results or not work at all.