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  • Title: [Preparative separation of the tryptic hydrolysate of a protein by high-pressure liquid chromatography. The primary structure of a monoclonal L-chain of k-type, subgroup I (Bence-Jones Protein Wes) (author's transl)].
    Author: Kratzin H, Yang CY, Krusche JU, Hilschmann N.
    Journal: Hoppe Seylers Z Physiol Chem; 1980 Oct; 361(10):1591-8. PubMed ID: 6778806.
    Abstract:
    The tryptic hydrolysate of Bence-Jones protein Wes (Mr = 23000) was separated by high-pressure liquid chromatography in a volatile buffer system on a reversed-phase column. From the resulting 22 peptides 18 yielded integer numbers after amino acid analysis. They could be used directly for a modified Edman degradation. Two peptides were not separated by this procedure, two were missing. Under different conditions these four peptides could also be prepared in pure form. 3 mg was sufficient to elucidate the primary structure of the variable part of this protein completely. The arrangement of the tryptic peptides was deduced by homology to other k=chains. Protein Wes contains 214 residues and belongs to subgroup I of the k-chains. The valine residue in position 191 indicates that it belongs to allotype Inv b+.
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