We have ~50 kD proteins in 13% PAGE that needs to be CNBr cleaved and
fragment extracted. The fragments of interest will be 8000 Daltons and
10,000 Daltons. Are there simple and reliable protocols for dissolving the
cleavage, dissolving the gel, extraction, partially purifying it (Z tip?)?
I've tried 23 hour trypsin treatment (2 ng trypsin for 3 gel slices) and
have only got partial digestion on the reduced proteins.
David T. Chin, Ph.D.
Director
Protein Biotechnology Core Facility
Univ. of Missouri - Columbia
Office: 573-882-2027
Lab. and Fax: 573-882-7105
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