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The Unblocked N-Terminal Sequence of Chicken IgG -Like Light Chains¹

From the Department of Microbiology and the Department of Biochemistry and Biophysics, University of Hawaii, Honolulu, Hawaii 96822

Abstract

The light chains of human and mouse immunoglobulins belong to two antigenically and chemically distinct classes, and (1, 2). Hood et al. (3) have suggested that the light chains of the immunoglobulins of other animal species can be classified as homologues of the and/or classes and that the ratios of to are variable among the species. The class has a free (unblocked) N-terminal amino acid and a C-terminal cysteine residue, whereas light chains of the class generally have a blocked N-terminal position, usually pyrrolid-2-one-5-carboxylic acid (PCA), and a penultimate cysteine residue at the C-terminal end (3, 4).

Light chains of both and classes have a unique structural feature: a variable region of about 107 amino acid residues in the N-terminal half of the light chain, and a common region of approximately residues 108 to 215.

Footnotes

¹ This investigation was supported in part by Research Grant AI-05660-06 and Training Grant AI-00243-07 from the National Institute of Allergy and Infectious Diseases.