Precursor sequence of MOPC-315 mouse immunoglobulin heavy and light chains

Partially purified mRNA coding for the MOPC-315 heavy (alpha) or light (lambda 2) immunoglobulin chain was translated in a nuclease-treated reticulocyte lysate containing 20 labeled amino acids. Radiolabeled precursor heavy and light chains, purified by immunoprecipitation and preparative gel electr...

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Bibliographic Details
Published in:The Journal of biological chemistry 1979-09, Vol.254 (18), p.9270-9276
Main Authors: Jilka, R L, Pestka, S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Cell Line
Immunoglobulin Heavy Chains - biosynthesis
Immunoglobulin Light Chains - biosynthesis
Mice
Peptide Fragments - analysis
Plasmacytoma
Protein Biosynthesis
Reticulocytes - metabolism
RNA, Messenger - metabolism
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Summary:Partially purified mRNA coding for the MOPC-315 heavy (alpha) or light (lambda 2) immunoglobulin chain was translated in a nuclease-treated reticulocyte lysate containing 20 labeled amino acids. Radiolabeled precursor heavy and light chains, purified by immunoprecipitation and preparative gel electrophoresis, were subjected to Edman degradation. The labeled phenylthiohydantoin derivatives obtained in each degradative cycle were identified and quantitated by high pressure liquid chromatography. Both heavy and light chain precursor segments were hydrophobic in nature; however, they were not homolgous in sequence. To establish whether COOH-terminal proteolytic processing of the heavy chain might also be occurring during secretion, the cyanogen bromide peptides of the heavy chain precursor were compared to those of the mature secreted heavy chain. The results indicated that the COOH termini of the two chains were identical.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)86840-0