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. 1969 Sep;64(1):381–387. doi: 10.1073/pnas.64.1.381

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

Charles J Sherr 1,2,†, Jonathan W Uhr 1,2
PMCID: PMC286173  PMID: 5263020

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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