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2L2 and
L1From the Department of Microbiology, The University of Texas Health Science Center at Dallas, Dallas, Texas 75235
Abstract
Murine cell surface immunoglobulin (Ig) isotypes were analyzed by lactoperoxidase-catalyzed radioiodination, immunoprecipitation, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). SDS-PAGE analysis revealed three radioactive peaks: I) IgM (µ2L2; 224,000 daltons), II) IgD (
2L2; 185,000 daltons), and III) IgD half-molecules (
L; 105,000 daltons). The size of the
-chain obtained from both the
2L2 and the
L molecules was the same (68,000 daltons). The
L molecules are apparently not the result of a sulfhydryl-catalyzed reduction or disulfide interchange and are probably not generated by proteolysis, since addition of alkylating agents and protease inhibitors did not decrease the amount of
L observed. Addition of sulfhydryl-oxidizing agents also did not decrease the amount of
L, suggesting that the
L molecules cannot be reoxidized to yield
2L2 molecules. The percentage of IgD in the
L form present on lymph node and spleen cells of A/J mice and on spleen cells of BALB/c mice was the same (
55%). The percentage of
L on splenocytes from BDF/1 mice (2 to 7 months old) was
42%. Spleen cells from strains that are "IgD-deficient," CBA/N and NZB, and spleen cells from 2-week-old BDF/1 mice, which have a low
/µ ratio, displayed a coordinate decrease in the levels of both
2L2 and
L. This coordinate decrease resulted in no alternation in the percentage of IgD present in the
L form (
42%). These results, taken together, indicate that indeed the cell surface Ig of murine lymphoid cell populations consists of monomeric IgM, monomeric IgD, and IgD half-molecules.
Footnotes
1 This work was supported by United States Public Health Service Grant AI 11851.
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