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Lyt-2 glycoprotein is synthesized as a single molecular species

We investigated the possibility that the Lyt-2 molecules made by uncloned mouse T lymphocytes would show variable primary structures like those of immunoglobulins. Newly synthesized Lyt-2/3 complexes were found to include only two major components, both discrete glycoproteins with apparent molecular...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2186898/
https://www.ncbi.nlm.nih.gov/pubmed/6848621
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description We investigated the possibility that the Lyt-2 molecules made by uncloned mouse T lymphocytes would show variable primary structures like those of immunoglobulins. Newly synthesized Lyt-2/3 complexes were found to include only two major components, both discrete glycoproteins with apparent molecular weights of 31,000 (31 K) and 35,000 (35 K). When products of Lyt-2.1 and Lyt-2.2 thymocytes were compared by two- dimensional nonequilibrium pH gradient electrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis, the isoelectric points of the 35 K molecules were different; thus, the 35 K component was likely to be encoded by the Lyt-2 locus itself. However, the 35 K molecules made by any one genotype were homogeneous in charge as well as in size. The homogeneity was obscured rapidly by post-translational modification. Most strikingly, within 30 min of initial synthesis, these processing events generated the conspicuous array of microheterogeneous products that form the "38 K" component of cell- surface Lyt-2/3.
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spelling pubmed-21868982008-04-17 Lyt-2 glycoprotein is synthesized as a single molecular species J Exp Med Articles We investigated the possibility that the Lyt-2 molecules made by uncloned mouse T lymphocytes would show variable primary structures like those of immunoglobulins. Newly synthesized Lyt-2/3 complexes were found to include only two major components, both discrete glycoproteins with apparent molecular weights of 31,000 (31 K) and 35,000 (35 K). When products of Lyt-2.1 and Lyt-2.2 thymocytes were compared by two- dimensional nonequilibrium pH gradient electrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis, the isoelectric points of the 35 K molecules were different; thus, the 35 K component was likely to be encoded by the Lyt-2 locus itself. However, the 35 K molecules made by any one genotype were homogeneous in charge as well as in size. The homogeneity was obscured rapidly by post-translational modification. Most strikingly, within 30 min of initial synthesis, these processing events generated the conspicuous array of microheterogeneous products that form the "38 K" component of cell- surface Lyt-2/3. The Rockefeller University Press 1983-01-01 /pmc/articles/PMC2186898/ /pubmed/6848621 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Lyt-2 glycoprotein is synthesized as a single molecular species
title Lyt-2 glycoprotein is synthesized as a single molecular species
title_full Lyt-2 glycoprotein is synthesized as a single molecular species
title_fullStr Lyt-2 glycoprotein is synthesized as a single molecular species
title_full_unstemmed Lyt-2 glycoprotein is synthesized as a single molecular species
title_short Lyt-2 glycoprotein is synthesized as a single molecular species
title_sort lyt-2 glycoprotein is synthesized as a single molecular species
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2186898/
https://www.ncbi.nlm.nih.gov/pubmed/6848621