| Literature DB >> 4207389 |
H R Morris, K E Batley, N C Harding, R A Bjur, J G Dann, R W King.
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.Entities:
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Year: 1974 PMID: 4207389 PMCID: PMC1166130 DOI: 10.1042/bj1370409
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857