Primary and secondary variants in immunoglobulin heavy chain production

Nature ◽  
1976 ◽  
Vol 264 (5585) ◽  
pp. 480-482 ◽  
Author(s):  
SAIJA KOSKIMIES ◽  
BARBARA K. BIRSHTEIN
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin Heavy Chain ◽  
Secondary Variants

scholarly journals Isolation and characterization of a variant of mouse plasmacytoma J558 synthesizing a 110,000-dalton immunoglobulin heavy chain and of secondary variants synthesizing either a 55,000-dalton or an 80,000-dalton immunoglobulin heavy chain: possible implications.

1982 ◽  
Vol 2 (9) ◽  
pp. 1134-1144 ◽  
Author(s):  
L Matsuuchi ◽  
S L Morrison
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin Heavy Chain ◽  
Immunoglobulin Gene ◽  
Wild Type ◽  
Covalent Bonds ◽  
In Vitro Synthesis ◽  
Heavy Chains ◽  
Isolation And Characterization ◽  
Secondary Variants

A mutant has been isolated from the J558 (immunoglobulin A, lambda, anti-alpha 1 leads to 3 dextran) cell line which synthesizes a heavy-chain immunoglobulin twice the size of normal heavy chain. Secondary variants that synthesized heavy chains either 1.5 times as large as wild type or the same size as wild type were identified. All mutants were serologically immunoglobulin continued to bind antigen, and retained the individual idiotype of the parent. Northern blot analysis and in vitro synthesis studies showed that the large heavy chains were primary synthetic products and not the consequence of abnormal covalent bonds. Cleavage of genomic DNA with restriction endonucleases and molecular hybridization studies showed new fragments in the 2 X and 1.5 X mutants which disappeared in the 1 X revertant. These data cannot easily be reconciled with the mutants arising either by unequal recombination or gene conversion. Further molecular characterization of these mutants should give additional insight into immunoglobulin gene evolution.

Isolation and characterization of a variant of mouse plasmacytoma J558 synthesizing a 110,000-dalton immunoglobulin heavy chain and of secondary variants synthesizing either a 55,000-dalton or an 80,000-dalton immunoglobulin heavy chain: possible implications

1982 ◽  
Vol 2 (9) ◽  
pp. 1134-1144
Author(s):  
L Matsuuchi ◽  
S L Morrison
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin Heavy Chain ◽  
Immunoglobulin Gene ◽  
Wild Type ◽  
Covalent Bonds ◽  
In Vitro Synthesis ◽  
Heavy Chains ◽  
Isolation And Characterization ◽  
Secondary Variants

A mutant has been isolated from the J558 (immunoglobulin A, lambda, anti-alpha 1 leads to 3 dextran) cell line which synthesizes a heavy-chain immunoglobulin twice the size of normal heavy chain. Secondary variants that synthesized heavy chains either 1.5 times as large as wild type or the same size as wild type were identified. All mutants were serologically immunoglobulin continued to bind antigen, and retained the individual idiotype of the parent. Northern blot analysis and in vitro synthesis studies showed that the large heavy chains were primary synthetic products and not the consequence of abnormal covalent bonds. Cleavage of genomic DNA with restriction endonucleases and molecular hybridization studies showed new fragments in the 2 X and 1.5 X mutants which disappeared in the 1 X revertant. These data cannot easily be reconciled with the mutants arising either by unequal recombination or gene conversion. Further molecular characterization of these mutants should give additional insight into immunoglobulin gene evolution.

scholarly journals Rhesus and cynomolgus macaque immunoglobulin heavy-chain genotyping yields comprehensive databases of germline VDJ alleles

Immunity ◽  
2021 ◽  
Vol 54 (2) ◽  
pp. 355-366.e4
Author(s):  
Néstor Vázquez Bernat ◽  
Martin Corcoran ◽  
Izabela Nowak ◽  
Mateusz Kaduk ◽  
Xaquin Castro Dopico ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Cynomolgus Macaque ◽  
Immunoglobulin Heavy Chain
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