Enzymatic digestion on the sample foil as a method for sequence determination by plasma desorption mass spectrometry: the primary structure of porpoise relaxin

Amina S. Woods, Robert J. Cotter, Motoi Yoshioka, Erika Büllesbach, Christian Schwabe

Research output: Contribution to journalArticlepeer-review

Abstract

Plasma desorption mass spectrometry (PDMS) was used to determine the C-terminus of the B-chain porpoise relaxin, a polypeptide hormone having three dimensional and disulfide homology with insulin. Trypsin was used to generate a series of peptide fragments for mapping by PDMS. The C-terminal fragments were purified and their sequences determined by on-foil digestion with carboxypeptidase Y.

Original languageEnglish (US)
Pages (from-to)77-88
Number of pages12
JournalInternational Journal of Mass Spectrometry and Ion Processes
Volume111
Issue numberC
DOIs
StatePublished - Dec 16 1991

ASJC Scopus subject areas

  • Spectroscopy

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