PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE : II. IMMUNOGLOBULINS IN THE PRIMARY IMMUNE RESPONSE OF THE BULLFROG, RANA CATESBIANA

The anuran amphibian, Rana catesbiana, has been found to possess at least two kinds of immunoglobulins corresponding to γG- and γM-classes. These classes have the same chain structures as those of their counterparts in higher animal species. Light chains of both immunoglobulins had molecular weight...

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Main Authors: Marchalonis, J., Edelman, G. M.
Format: Online
Language:English
Published: The Rockefeller University Press 1966
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138259/
id pubmed-2138259
recordtype oai_dc
spelling pubmed-21382592008-04-17 PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE : II. IMMUNOGLOBULINS IN THE PRIMARY IMMUNE RESPONSE OF THE BULLFROG, RANA CATESBIANA Marchalonis, J. Edelman, G. M. Article The anuran amphibian, Rana catesbiana, has been found to possess at least two kinds of immunoglobulins corresponding to γG- and γM-classes. These classes have the same chain structures as those of their counterparts in higher animal species. Light chains of both immunoglobulins had molecular weights of 20,000. Heavy chains of the γM-class had molecular weights of 72,100; those of the γG-class had molecular weights of 53,600. The carbohydrate content of the γG-immunoglobulin was 2.1%, and that of the γM-protein was 10.8%. The amino acid compositions of the immunoglobulins were generally similar to those of mammalian immunoglobulins. After a single injection of phage antigen (f2), the order of appearance of phage-neutralizing activity in the frog immunoglobulin classes was (a) γM-antibodies, and (b) γG-antibodies. The results of this and previous studies suggest that the γG-immunoglobulins emerged at some point in evolution between the elasmobranchs and the anuran amphibians. The Rockefeller University Press 1966-10-31 /pmc/articles/PMC2138259/ /pubmed/4162734 Text en Copyright © 1966 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Marchalonis, J.
Edelman, G. M.
spellingShingle Marchalonis, J.
Edelman, G. M.
PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE : II. IMMUNOGLOBULINS IN THE PRIMARY IMMUNE RESPONSE OF THE BULLFROG, RANA CATESBIANA
author_facet Marchalonis, J.
Edelman, G. M.
author_sort Marchalonis, J.
title PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE : II. IMMUNOGLOBULINS IN THE PRIMARY IMMUNE RESPONSE OF THE BULLFROG, RANA CATESBIANA
title_short PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE : II. IMMUNOGLOBULINS IN THE PRIMARY IMMUNE RESPONSE OF THE BULLFROG, RANA CATESBIANA
title_full PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE : II. IMMUNOGLOBULINS IN THE PRIMARY IMMUNE RESPONSE OF THE BULLFROG, RANA CATESBIANA
title_fullStr PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE : II. IMMUNOGLOBULINS IN THE PRIMARY IMMUNE RESPONSE OF THE BULLFROG, RANA CATESBIANA
title_full_unstemmed PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE : II. IMMUNOGLOBULINS IN THE PRIMARY IMMUNE RESPONSE OF THE BULLFROG, RANA CATESBIANA
title_sort phylogenetic origins of antibody structure : ii. immunoglobulins in the primary immune response of the bullfrog, rana catesbiana
description The anuran amphibian, Rana catesbiana, has been found to possess at least two kinds of immunoglobulins corresponding to γG- and γM-classes. These classes have the same chain structures as those of their counterparts in higher animal species. Light chains of both immunoglobulins had molecular weights of 20,000. Heavy chains of the γM-class had molecular weights of 72,100; those of the γG-class had molecular weights of 53,600. The carbohydrate content of the γG-immunoglobulin was 2.1%, and that of the γM-protein was 10.8%. The amino acid compositions of the immunoglobulins were generally similar to those of mammalian immunoglobulins. After a single injection of phage antigen (f2), the order of appearance of phage-neutralizing activity in the frog immunoglobulin classes was (a) γM-antibodies, and (b) γG-antibodies. The results of this and previous studies suggest that the γG-immunoglobulins emerged at some point in evolution between the elasmobranchs and the anuran amphibians.
publisher The Rockefeller University Press
publishDate 1966
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138259/
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