Amino acid sequence analysis of immunoglobulin light chains by gas chromatographic-mass spectrometric techniques

Structural identity of nominal and latent b9 molecules

Martin Yarmush, Henry C. Krutzsch, Thomas J. Kindt

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Light chains with latent allotype b9 were isolated by immunoabsorbent techniques from serum samples taken from a pedigreed rabbit with allotype b4b4. Amino acid sequence data obtained for the NH2 terminus of the constant region of these light chains, following acid cleavage of the aspartyl-proline bond at positions 109-110, revealed an NH2 terminal Sequence characteristic of nominal b9 light chains. The analyses utilized gas chromatography-mass spectrometry to identify dipeptides obtained by digestion of the modified light chains with dipeptidylaminopeptidases I and IV. Similar examinations of b4 light chains revealed significant differences from b9 in the dipeptides obtained. These data provide evidence that light chains bearing latent allotype markers are structurally indistinguishable from those expressed as nominal allotypes.

Original languageEnglish (US)
Pages (from-to)319-326
Number of pages8
JournalMolecular Immunology
Volume17
Issue number3
DOIs
StatePublished - Jan 1 1980
Externally publishedYes

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Immunoglobulin Light Chains
Protein Sequence Analysis
Gases
Light
Dipeptides
aspartyl-proline
Gas Chromatography-Mass Spectrometry
Digestion
Amino Acid Sequence
Rabbits
Acids
Serum

All Science Journal Classification (ASJC) codes

  • Immunology
  • Molecular Biology

Cite this

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abstract = "Light chains with latent allotype b9 were isolated by immunoabsorbent techniques from serum samples taken from a pedigreed rabbit with allotype b4b4. Amino acid sequence data obtained for the NH2 terminus of the constant region of these light chains, following acid cleavage of the aspartyl-proline bond at positions 109-110, revealed an NH2 terminal Sequence characteristic of nominal b9 light chains. The analyses utilized gas chromatography-mass spectrometry to identify dipeptides obtained by digestion of the modified light chains with dipeptidylaminopeptidases I and IV. Similar examinations of b4 light chains revealed significant differences from b9 in the dipeptides obtained. These data provide evidence that light chains bearing latent allotype markers are structurally indistinguishable from those expressed as nominal allotypes.",
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Amino acid sequence analysis of immunoglobulin light chains by gas chromatographic-mass spectrometric techniques : Structural identity of nominal and latent b9 molecules. / Yarmush, Martin; Krutzsch, Henry C.; Kindt, Thomas J.

In: Molecular Immunology, Vol. 17, No. 3, 01.01.1980, p. 319-326.

Research output: Contribution to journalArticle

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AU - Yarmush, Martin

AU - Krutzsch, Henry C.

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