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- W4313311024 abstract "Abstract Protein 315 (the A-myeloma protein produced by MOPC-315) binds ε-DNP-lysine and menadione with high affinity (1 × 107 M-1 and 5 × 105 M-1, respectively, at 4°C). Over 90% of residues of the light chain of this protein (L315) have been sequenced by E. Schulenburg, E. Simms, R. Bradshaw and H. Eisen. Of the residues in the C-terminal half, 30% differ from the corresponding residues of the MOPC-104 light chain (L104) and about 65% differ from those of mouse κ chains. In its N-terminal half, L315 differs in only about 10% of the residues from L104. A rabbit antiserum specific for L315 has been prepared by R. Lynch and used in a double antibody assay (125I-315 plus rabbit anti-L315 plus goat anti-rabbit Fc) to demonstrate L315-like chains in normal sera from BALB/c and C57BC/6 mice. Both sera contained these chains at the same low level, about 0.02% to 0.1% of the total immunoglobulin." @default.
- W4313311024 created "2023-01-06" @default.
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- W4313311024 date "1971-09-01" @default.
- W4313311024 modified "2023-10-14" @default.
- W4313311024 title "Studies on the γA Protein from MOPC-315" @default.
- W4313311024 doi "https://doi.org/10.4049/jimmunol.107.3.924.b" @default.
- W4313311024 hasPublicationYear "1971" @default.
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