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- W2046250344 abstract "Chicken antisera to mouse myeloma IgM can precipitate specifically Ig-like components obtained from surface iodinated and detergent lysed thymocytes. When these immunoprecipitates were dissolved in SDS/urea, reduced, and alkylated, four peptide species could be separated in polyacrylamide electrophoresis, one of which had the mobility of a μ chain, two others being much larger (> 1000,000), and the fourth migrating between γ and L chains. It is suspected that much of the surface Ig is irreversibly aggregated and that the observed peptides represent oligomers of smaller units. The tendency to oligomerize was lessened in gel filtration using 6 M guanidine. Under these conditions, a peptide chain of 22,000 daltons (P22) in range with an L chain, a peptide of 71,000 daltons (P71) compatible with a μ chain, on unidentified intermediate peptide, and one peptide of > 100,000 daltons were obtained. On isolation and gel electrophoresis, P71 coincided with a μ chain, but P22 was located between the L and γ marker, possibly having been dimerized. In further experiments designed to demonstrate the presence of μ-determinants on thymocytes and to exclude in the antiserum contaminating antibodies as the agents responsible for the fluorescence reaction, thymocytes were saturated with chicken anti-IgM and subsequently eluted at pH 2.0. Eluted antibody was entirely IgM speficic as demonstrated by its capacity to precipitate 125I labeled IgM, but not of mouse IgG. The involvement of cytophilic immunoglobulin was excluded by the fact that rabbit anti-IgM and chicken anti-IgG yielded much less active eluates. Furthermore, analysis by polyacrylamide gel electrophoresis showed that the radioactivity precipitated by eluates of anti-IgM treated cell was virtually all associated with IgM." @default.
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- W2046250344 date "2009-10-01" @default.
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- W2046250344 title "P75 A promising method for visualization of immune responses in immunoproteomics" @default.
- W2046250344 doi "https://doi.org/10.1016/s1359-6349(09)72229-3" @default.
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