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    FEBS Lett. 1988 Mar 14;229(2):265-72.

    A new strategy for primary structure determination of proteins: application to bovine beta-casein.

    Carles C, Huet JC, Ribadeau-Dumas B.

    Institut National de la Recherche Agronomique, CRJ, Jouy-en-Josas, France.

    A new approach has been developed for sequencing proteins. A radioactive label is attached specifically to the C-terminus of the protein. The labelled molecule is subjected to varying proteolysis conditions. From the electrophoretic patterns (SDS-PAGE) of the hydrolysates, appropriate cleavage conditions are selected, giving labelled peptides of different lengths which are purified. The labelled peptides are sequenced in order of increasing size (from 1 to n), peptide (i) being sequenced until the N-terminal sequence of peptide (i-1) is encountered. This approach allows the determination of a complete protein sequence with a minimal number of Edman cycles. The method was successfully applied to bovine beta-casein (209 residues) which was completely resequenced with only 239 Edman cycles.

    PMID: 3278933 [PubMed - indexed for MEDLINE]

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