| Literature DB >> 9406186 |
Abstract
Detailed procedures are described for successfully digesting reasonably small quantities (i.e., usually > 10 pmol) of proteins with a variety of proteases and for then isolating the resulting peptides by reverse-phase HPLC. Since sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) appears to be the current method of choice for final purification of proteins for structural analysis, special attention is given to carrying out in-gel proteolytic digests on SDS-PAGE-separated proteins that have usually been stained with Coomassie Blue. A compilation of data from nearly 200 "unknown" samples is used to help provide realistic expectations with respect to the results that are likely to be obtained from carrying out in-gel proteolytic digests on large numbers of proteins.Entities:
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Year: 1997 PMID: 9406186 DOI: 10.1007/BF02752260
Source DB: PubMed Journal: Mol Biotechnol ISSN: 1073-6085 Impact factor: 2.695