Recombinant rabbit secretory immunoglobulin molecules: alpha chains with maternal (paternal) variable region allotypes and paternal (maternal) constant region allotypes

K. L. Knight, Thomas Malek, W. C. Hanly

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

A population of IgA molecules having heavy chains coded by two parental chromosomes in trans position was identified in rabbits heterozygous at both the V(H)a locus, which controls allotypic specificities on the variable part of heavy chains, and the C(α)g locus, which controls allotypic specificities on the constant part of alpha chains. These recombinant molecules have alpha chain allotypic specificities controlled by both the maternal V(H)a gene and the paternal C(α)g gene or conversely, the paternal V(H)a gene and the maternal C(α)g gene. These recombinant molecules were found in F(ab)(2α) fractions obtained after passage of F(ab)(2α) preparations through immunosorbent columns designed to remove one population of F(ab)(2α) molecules, i.e., g74 or g75 type molecules. The effluent F(ab)(2α) fractions were then examined by radio precipitation methods for allotypic specificities controlled by the V(H)a and C(α)g loci. About 40% of the g75 F(ab)2α) molecules from each of three rabbits with the a1g74 and a2g75 allogroups were alg75 recombinants. These alg75 recombinant molecules represented from 2.5-5.6% of the total unfractionated F(ab)(2α) sample. The F(ab)(2α) fractions from two rabbits with the a1g75 and a3g74 allogroups had from 1.8-8.2% recombinant molecules: some were alg74 recombinants and some were a3g75 recombinants. Somatic recombination as a mechanism responsible for the synthesis of polypeptide chains in which part of the information is obtained from one chromosome and part from the homologous chromosome is discussed.

Original languageEnglish
Pages (from-to)1169-1173
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume71
Issue number4
StatePublished - Dec 1 1974
Externally publishedYes

Fingerprint

Immunoglobulin alpha-Chains
Mothers
Rabbits
Internal-External Control
Chromosomes
Genes
Immunosorbents
Radio
Immunoglobulin A
Genetic Recombination
Population
Peptides

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

@article{6c19e73e2ea24ff5870d2a89c632568f,
title = "Recombinant rabbit secretory immunoglobulin molecules: alpha chains with maternal (paternal) variable region allotypes and paternal (maternal) constant region allotypes",
abstract = "A population of IgA molecules having heavy chains coded by two parental chromosomes in trans position was identified in rabbits heterozygous at both the V(H)a locus, which controls allotypic specificities on the variable part of heavy chains, and the C(α)g locus, which controls allotypic specificities on the constant part of alpha chains. These recombinant molecules have alpha chain allotypic specificities controlled by both the maternal V(H)a gene and the paternal C(α)g gene or conversely, the paternal V(H)a gene and the maternal C(α)g gene. These recombinant molecules were found in F(ab)(2α) fractions obtained after passage of F(ab)(2α) preparations through immunosorbent columns designed to remove one population of F(ab)(2α) molecules, i.e., g74 or g75 type molecules. The effluent F(ab)(2α) fractions were then examined by radio precipitation methods for allotypic specificities controlled by the V(H)a and C(α)g loci. About 40{\%} of the g75 F(ab)2α) molecules from each of three rabbits with the a1g74 and a2g75 allogroups were alg75 recombinants. These alg75 recombinant molecules represented from 2.5-5.6{\%} of the total unfractionated F(ab)(2α) sample. The F(ab)(2α) fractions from two rabbits with the a1g75 and a3g74 allogroups had from 1.8-8.2{\%} recombinant molecules: some were alg74 recombinants and some were a3g75 recombinants. Somatic recombination as a mechanism responsible for the synthesis of polypeptide chains in which part of the information is obtained from one chromosome and part from the homologous chromosome is discussed.",
author = "Knight, {K. L.} and Thomas Malek and Hanly, {W. C.}",
year = "1974",
month = "12",
day = "1",
language = "English",
volume = "71",
pages = "1169--1173",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "4",

}

TY - JOUR

T1 - Recombinant rabbit secretory immunoglobulin molecules

T2 - alpha chains with maternal (paternal) variable region allotypes and paternal (maternal) constant region allotypes

AU - Knight, K. L.

AU - Malek, Thomas

AU - Hanly, W. C.

PY - 1974/12/1

Y1 - 1974/12/1

N2 - A population of IgA molecules having heavy chains coded by two parental chromosomes in trans position was identified in rabbits heterozygous at both the V(H)a locus, which controls allotypic specificities on the variable part of heavy chains, and the C(α)g locus, which controls allotypic specificities on the constant part of alpha chains. These recombinant molecules have alpha chain allotypic specificities controlled by both the maternal V(H)a gene and the paternal C(α)g gene or conversely, the paternal V(H)a gene and the maternal C(α)g gene. These recombinant molecules were found in F(ab)(2α) fractions obtained after passage of F(ab)(2α) preparations through immunosorbent columns designed to remove one population of F(ab)(2α) molecules, i.e., g74 or g75 type molecules. The effluent F(ab)(2α) fractions were then examined by radio precipitation methods for allotypic specificities controlled by the V(H)a and C(α)g loci. About 40% of the g75 F(ab)2α) molecules from each of three rabbits with the a1g74 and a2g75 allogroups were alg75 recombinants. These alg75 recombinant molecules represented from 2.5-5.6% of the total unfractionated F(ab)(2α) sample. The F(ab)(2α) fractions from two rabbits with the a1g75 and a3g74 allogroups had from 1.8-8.2% recombinant molecules: some were alg74 recombinants and some were a3g75 recombinants. Somatic recombination as a mechanism responsible for the synthesis of polypeptide chains in which part of the information is obtained from one chromosome and part from the homologous chromosome is discussed.

AB - A population of IgA molecules having heavy chains coded by two parental chromosomes in trans position was identified in rabbits heterozygous at both the V(H)a locus, which controls allotypic specificities on the variable part of heavy chains, and the C(α)g locus, which controls allotypic specificities on the constant part of alpha chains. These recombinant molecules have alpha chain allotypic specificities controlled by both the maternal V(H)a gene and the paternal C(α)g gene or conversely, the paternal V(H)a gene and the maternal C(α)g gene. These recombinant molecules were found in F(ab)(2α) fractions obtained after passage of F(ab)(2α) preparations through immunosorbent columns designed to remove one population of F(ab)(2α) molecules, i.e., g74 or g75 type molecules. The effluent F(ab)(2α) fractions were then examined by radio precipitation methods for allotypic specificities controlled by the V(H)a and C(α)g loci. About 40% of the g75 F(ab)2α) molecules from each of three rabbits with the a1g74 and a2g75 allogroups were alg75 recombinants. These alg75 recombinant molecules represented from 2.5-5.6% of the total unfractionated F(ab)(2α) sample. The F(ab)(2α) fractions from two rabbits with the a1g75 and a3g74 allogroups had from 1.8-8.2% recombinant molecules: some were alg74 recombinants and some were a3g75 recombinants. Somatic recombination as a mechanism responsible for the synthesis of polypeptide chains in which part of the information is obtained from one chromosome and part from the homologous chromosome is discussed.

UR - http://www.scopus.com/inward/record.url?scp=0016238913&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016238913&partnerID=8YFLogxK

M3 - Article

C2 - 4133846

AN - SCOPUS:0016238913

VL - 71

SP - 1169

EP - 1173

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 4

ER -