Dihydrofolate reductase: low-resolution mass-spectrometric analysis of an elastase digest as a sequencing tool (Short Communication) |
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Authors: | Howard R. Morris Karen E. Batley Nigel G. L. Harding Richard A. Bjur John G. Dann Rodney W. King |
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Affiliation: | University Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, U.K.;Postgraduate Medical School, University of Cambridge, Hills Road, Cambridge CB2 2QL, U.K.;National Institute for Medical Research, Mill Hill, London NW7 1AA, U.K. |
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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. |
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