@article{f0bab1e3cda54aaba201621485981c54,
title = "N-terminal sequence heterogeneity of guinea pig anti-DNP kappa chains",
abstract = "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.",
author = "Grant, {J. A.} and Lamm, {M. E.} and L. Hood",
note = "Funding Information: J. A. GRANT, M. E. LAMMt and L. HOOD Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland and Department of Pathology, New York University School of Medicine, New York, N.Y. 10016, U.S.A. Funding Information: Anti-DNP antibody was prepared, purified and the light chains isolated as previously described \[4, 10\]. Normal guinea pig light chains were isolated from Pentex gamma globulin \[3\].T he control protein (Hac), a homogeneous human Bence Jones kappa chain, was purified by DEAE cellulose chromatography. The light chains were performic acid oxidized\[11\]a nd submitted to the three- *This investigation was supported in part by Grant No. E-427A, a Marion Dunlap Colvin Memorial Grant, fi'om the American Cancer Society. tRecipient of a Career Scientist Award of the Health Research Council of the City of New York under Contract No. 1-474.",
year = "1969",
month = sep,
doi = "10.1016/0019-2791(67)90129-2",
language = "English (US)",
volume = "6",
pages = "645--648",
journal = "Immunochemistry",
issn = "0019-2791",
publisher = "Elsevier Limited",
number = "5",
}