Amino acid sequence analysis of immunoglobulin light chains by gas chromatographic-mass spectrometric techniques: Structural identity of nominal and latent b9 molecules

Martin L. Yarmush; Henry C. Krutzsch; Thomas J. Kindt

doi:10.1016/0161-5890(80)90052-8

Amino acid sequence analysis of immunoglobulin light chains by gas chromatographic-mass spectrometric techniques: Structural identity of nominal and latent b9 molecules

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

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

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 language	English (US)
Pages (from-to)	319-326
Number of pages	8
Journal	Molecular Immunology
Volume	17
Issue number	3
DOIs	https://doi.org/10.1016/0161-5890(80)90052-8
State	Published - Mar 1980
Externally published	Yes

All Science Journal Classification (ASJC) codes

Immunology
Molecular Biology

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10.1016/0161-5890(80)90052-8

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title = "Amino acid sequence analysis of immunoglobulin light chains by gas chromatographic-mass spectrometric techniques: Structural identity of nominal and latent b9 molecules",

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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year = "1980",

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T1 - Amino acid sequence analysis of immunoglobulin light chains by gas chromatographic-mass spectrometric techniques

T2 - Structural identity of nominal and latent b9 molecules

AU - Yarmush, Martin L.

AU - Krutzsch, Henry C.

AU - Kindt, Thomas J.

PY - 1980/3

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N2 - 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.

AB - 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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