Gross conformation of free polypeptide chains from rabbit immunoglobulin G. II. Light chain

Biochemistry ◽  
1971 ◽  
Vol 10 (8) ◽  
pp. 1280-1288 ◽  
Author(s):  
Charles Tanford ◽  
Ingemar Bjork
1968 ◽  
Vol 107 (4) ◽  
pp. 449-453 ◽  
Author(s):  
E. Rüde ◽  
D. Givol

The light chain of rabbit immunoglobulin G was shown to contain 15–20% blocked N-terminal residue. The blocked residue is pyrrolid-2-one-5-carboxylic acid, and most of the chains that contain this residue have the N-terminal sequence pyrrolid-2-one-5-carbonyl-valine.


Hereditas ◽  
2008 ◽  
Vol 98 (1) ◽  
pp. 83-87 ◽  
Author(s):  
H. A. SUOMALAINEN ◽  
L. BRYS ◽  
W. VAN DER LOO ◽  
J. SCHRÖDER

1982 ◽  
Vol 156 (2) ◽  
pp. 585-595 ◽  
Author(s):  
A Benammar ◽  
P A Cazenave

Immunoglobulin G (IgG) from the rabbit strain Basilea was previously shown to contain two distinct populations of molecules one with light chain belonging to the known lambda isotype and the others to a new kappa-like L chain type. Alloantisera prepared against the Basilea IgG are directed against the kappa-like light chain (anti-bas antisera). All Basilea rabbits express kappa-like chains recognized by anti-bas sera, but IgG from other domestic rabbits did not react with these antisera. Genetic studies of wild rabbits belonging to different populations show that the bas+ phenotype could be found in heterozygous rabbits as well as those homozygous at the b locus. The gene encoding the bas+ light chain is closely linked to the b locus. Moreover, antigenic determinants recognized by anti-bas antibodies and antigenic determinants recognized by antibodies directed against allotypic determinants of the b series are located on distinct IgG molecules. These results show that there are two rabbit kappa isotypes: the kappa 1 isotype, bearing allotypic determinants of the b series, and the kappa 2 isotype, for which bas+ chain is one of the allotypic forms. The kappa 1 and kappa 2 isotypes are controlled by closely linked genes.


2007 ◽  
Vol 22 (12) ◽  
pp. 2884-2890 ◽  
Author(s):  
Elisabeth Briand ◽  
Michèle Salmain ◽  
Chantal Compère ◽  
Claire-Marie Pradier

1984 ◽  
Vol 159 (4) ◽  
pp. 1096-1104 ◽  
Author(s):  
M Taniguchi ◽  
T Tokuhisa ◽  
T Itoh ◽  
M Kanno

The functional roles of the two polypeptide chains that compose the T cell suppressor factor (TsF) that mediates the antigen-specific and genetically restricted suppressor function were studied by using the heavy or light chains isolated from the conventional TsF or the 11S and 13S mRNA translation products of TsF. Either the heavy or the light chain of mRNA translation products reconstitutes the active TsF that suppresses the antibody response in an antigen-specific and genetically restricted manner when it is combined with the isolated heavy or light chain from the conventional TsF. As a consequence, the antigen-binding heavy chain mediates the antigen specificity of TsF. On the other hand, the I-J-positive light chain works as an element to determine the genetic restriction specificity. Thus, the identity of the histocompatibility between the I-J haplotypes on the light chain and the responding cell is essential for the functional expression of TsF. No genetic preference, however, was observed, in the association of the heavy and light chains of TsF.


1987 ◽  
Vol 7 (2) ◽  
pp. 936-939
Author(s):  
A Greenberg ◽  
R Ber ◽  
Z Kra-Oz ◽  
R Laskov

Adherent hybrids between immunoglobulin-producing mouse myeloma cells and fibroblasts do not produce immunoglobulin polypeptide chains. These hybrids retained the actively rearranged immunoglobulin genes of the myeloma parental cells but lacked immunoglobulin heavy- and light-chain RNA transcripts. We conclude that the shutoff of immunoglobulin production in these hybrids occurs at the transcription or early processing level.


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