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 | |
| State | Published - Jan 1 1980 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Immunology
- Molecular Biology
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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 journal › Article
TY - JOUR
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
AU - Krutzsch, Henry C.
AU - Kindt, Thomas J.
PY - 1980/1/1
Y1 - 1980/1/1
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.
UR - http://www.scopus.com/inward/record.url?scp=0018864057&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0018864057&partnerID=8YFLogxK
U2 - 10.1016/0161-5890(80)90052-8
DO - 10.1016/0161-5890(80)90052-8
M3 - Article
C2 - 6777661
AN - SCOPUS:0018864057
VL - 17
SP - 319
EP - 326
JO - Molecular Immunology
JF - Molecular Immunology
SN - 0161-5890
IS - 3
ER -