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.
|Number of pages
|International Journal of Mass Spectrometry and Ion Processes
|Published - Dec 16 1991
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