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• W2015736304 startingPage "2926" @default.
• W2015736304 abstract "The S107 myeloma cell line expresses the germ-line sequence of the T15 antiphosphocholine (P-Cho) antibody, which is the major antibody made by BALB/c mice in response to P-Cho, either on a variety of bacterial polysaccharides or when attached to a protein carrier. We have previously reported that a somatic mutant of the S107 cell line produces an antibody that has lost the ability to bind P-Cho and has acquired binding for double-stranded DNA. This antibody has a substitution of an alanine for a glutamic acid at residue 35 in the heavy chain variable region. We now show that this amino acid substitution is due to a single A-C transversion, which is the only nucleotide change in the heavy and light chain variable regions. Further, it appears that this change is due to somatic mutation rather than to gene conversion." @default.
• W2015736304 created "2016-06-24" @default.
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• W2015736304 date "1987-05-01" @default.
• W2015736304 modified "2023-10-02" @default.
• W2015736304 title "Somatic diversification of S107 from an antiphosphocholine to an anti-DNA autoantibody is due to a single base change in its heavy chain variable region." @default.
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• W2015736304 doi "https://doi.org/10.1073/pnas.84.9.2926" @default.
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