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Updated: Aug 3, 2026

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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
Published on: December 21, 2010
Dihydrofolate reductase: low-resolution mass-spectrometric analysis of an elastase digest as a sequencing tool
The Biochemical Journal
|February 1, 1974
Abstract:
An elastase digest of a protein of unknown structure, dihydrofolate reductase, was studied by mass spectrometry. This soluble digest contained a large number of small peptides in different yields, within the ideal molecular-weight range (200-1200) for mixture-analysis mass spectrometry. Sequences of the major component peptides in the digest are reported.

