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 Ishizaka, K. Articles by Tada, T. Search for Related Content PubMed Articles by Ishizaka, K. Articles by Tada, T.

Immunoglobulin E in the Monkey¹

From the Children's Asthma Research Institute and Hospital, Denver, Colorado

Abstract

An immunoglobulin reacting with anti-human E antibodies was detected in the sera of monkeys immunized with Ascaris antigen or infested with parasitic mites. The monkey protein gave a precipitin band with antiserum specific for the F_c portion of human E, but failed to react with any of the antisera specific for the other human immunoglobulin classes. The human E precipitin band showed a spur over the precipitin band formed between the monkey protein and anti-human E. The monkey protein reacted with anti-light chains, indicating that it is an immunoglobulin. The physicochemical properties of the protein, i.e., electrophoretic mobility, sedimentation coefficient and chromatographic characteristics, were similar to those of human E. It was also found that monkey homocytotropic antibodies against Ascaris antigen resided in the protein. These findings indicate that the monkey protein represents a distinct immunoglobulin class, corresponding to human E. E-forming cells were found in the lungs and regional lymph nodes of the animals infested with mites.

Footnotes

This work was supported mainly by Grants GB-4646 and GB-8370 from the National Science Foundation and partly by Grant AI-04985 from the United States Public Health Service.