HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Kubo, R. T. Articles by Benedict, A. A. Search for Related Content PubMed Articles by Kubo, R. T. Articles by Benedict, A. A.

Amino Terminal Sequences of Heavy and Light Chains of Chicken Anti-Dinitrophenyl Antibody¹

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

Abstract

Based on their amino terminal sequences human and light (L) chains form several subgroups (1–3). The L chains of the immunoglobulins of other animal species have been classified as homologues of the and/or classes (4). The class has been characterized as having a free (unblocked) amino terminus and a carboxyl terminal half cystine residue, whereas the class has been considered generally to have a blocked amino terminus, usually pyrrolidone carboxylic acid, and a penultimate half cystine residue at the carboxyl terminus (4, 5). Based on these criteria, Hood et al. (4) suggested that the chicken L chain was a type. Although the L chain from normal chicken IgG has an unblocked N-terminal amino acid (4, 6), we reported that the first 17 residues appeared to fit better in the N-terminal sequence of human rather than chains (6).

Footnotes

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