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Mouse myeloma cells were pulse-labeled in vitro with (3)H-D-glucosamine and (14)C-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 (3)H-glucosamine in labeled post-ribosomal material. Polyribosomes labeled with (3)H-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.

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