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Amino acid sequence of the precursor region of MOPC-315 mouse immunoglobulin heavy chain.
Author(s) -
Robert L. Jilka,
Sidney Pestka
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.12.5692
Subject(s) - edman degradation , amino acid , reticulocyte , immunoprecipitation , immunoglobulin heavy chain , peptide sequence , immunoglobulin light chain , microbiology and biotechnology , biochemistry , gel electrophoresis , antibody , chemistry , biology , messenger rna , gene , immunology
Partially purified mRNA coding for the MOPC-315 heavy immunoglobulin alpha chain was translated in a reticulocyte lysate containing 20 labeled amino acids. Radiolabeled MOPC-315 heavy chain precursor protein, purified by preparative gel electrophoresis and immunoprecipitation, was sequenced by Edman degradation. The labeled phenylthiohydantoin amino acid obtained in each cycle was identified and quantitated by high-pressure liquid chromatography. The precursor sequence of 18 amino acids, Met-Lys-Val-Leu-Ser-Leu-Leu-Tyr-Leu-Leu-Thr-Ala-Ile-Pro-His-Ile-Met-Ser, preceded the sequence corresponding to the NH2 terminus of the mature secreted heavy chain.

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