IMMUNOGLOBULIN SYNTHESIS AND SECRETION, III. INCORPORATION OF GLUCOSAMINE INTO IMMUNOGLOBULIN ON POLYRIBOSOMES*

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Mouse myeloma cells were pulse-labeled in vitro with 3H-D-glucosamine and 14C-L-leucine. Analysis on sucrose gradients revealed incorporation of both isotopes into polyribosomes and release of most of such radioactivity after treatment of labeled cells in vitro with puromycin. A mixing experiment excluded the in vitro binding to unlabeled polyribosomes of 3H-glucosamine in labeled post-ribosomal material. Polyribosomes labeled with 3H-glucosamine were precipitated with antiserum specific for mouse immunoglobulin. By chromatography and gel filtration, the precipitable radioactivity was shown to be glucosamine covalently bound to heavy and light chains.

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