The amino acids present at the first four N-terminal positions of light chains derived from guinea pig pooled normal immunoglobulins and a purified anti-DNP antibody were determined quantitatively. Light chains from both sources were heterogeneous, and the quantitative yields of predominant amino acids were similar. This indicates that the DNP determinant does not select for a single specificity region in the antibody light chains of guinea pigs. Qualitatively, the amino acids observed at each position were the same ones seen at the comparable positions of normal human light chains, suggesting the existence of guinea pig specificity region subclasses.
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