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Papers by David Hagins
Immunochemistry, 1977
The light chains of specifically purified antibodies to DNP-bovine gamma globulin (DNP-BGG) and D... more The light chains of specifically purified antibodies to DNP-bovine gamma globulin (DNP-BGG) and DNP-p-aminobenzoylglutamate-BGG (DNP-ABG-BGG) were isolated and their N-terminal amino acid sequences were determined. The amino acid composition at each locus of the N-terminus was quantitatively determined for 20 steps using high pressure liquid chromatographymass spectrometry to identify the amino acid phenylthiohydantoin derivatives isolated at each step from the automatic protein sequencer. In this manner it was observed that the N-terminal amino acid sequence of the anti-DNP antibody light chain preparation was at most loci essentially the same as that of the anti-DNP-ABG antibody light chain. It was also observed that both antibody L-chains were equally structurally heterogeneous, having a region near the N-terminus exhibiting hypervariability in the manner previously described for other rabbit L-chains. The variability and sequence homology between the two L-chain preparations are discussed in light of the composite sequence data published for other rabbit anti-hapten L-chains. "E © r~ olo O ¢.~ e-< z © ©
Immunochemistry, 1977
The light chains of specifically purified antibodies to DNP-bovine gamma globulin (DNP-BGG) and D... more The light chains of specifically purified antibodies to DNP-bovine gamma globulin (DNP-BGG) and DNP-p-aminobenzoylglutamate-BGG (DNP-ABG-BGG) were isolated and their N-terminal amino acid sequences were determined. The amino acid composition at each locus of the N-terminus was quantitatively determined for 20 steps using high pressure liquid chromatographymass spectrometry to identify the amino acid phenylthiohydantoin derivatives isolated at each step from the automatic protein sequencer. In this manner it was observed that the N-terminal amino acid sequence of the anti-DNP antibody light chain preparation was at most loci essentially the same as that of the anti-DNP-ABG antibody light chain. It was also observed that both antibody L-chains were equally structurally heterogeneous, having a region near the N-terminus exhibiting hypervariability in the manner previously described for other rabbit L-chains. The variability and sequence homology between the two L-chain preparations are discussed in light of the composite sequence data published for other rabbit anti-hapten L-chains. "E © r~ olo O ¢.~ e-< z © ©