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Membrane proteins synthesized by rabbit reticulocytes
Intact rabbit reticulocyte cells synthesize two predominant species of polypeptides which are components of the cell plasma membrane. Previous work (Lodish, H. F. 1973. Proc. Natl. Acad. Sci. U. S. A. 70:1526- 1530.) showed that these proteins were synthesized by polyribosomes not attached to membra...
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Lenguaje: | English |
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The Rockefeller University Press
1975
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111166/ https://www.ncbi.nlm.nih.gov/pubmed/1127015 |
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collection | PubMed |
description | Intact rabbit reticulocyte cells synthesize two predominant species of polypeptides which are components of the cell plasma membrane. Previous work (Lodish, H. F. 1973. Proc. Natl. Acad. Sci. U. S. A. 70:1526- 1530.) showed that these proteins were synthesized by polyribosomes not attached to membranes. We show here that both polypeptides are confined to the cytoplasmic surface of the cell membrane. These studies utilized iodination of whole cells and of membranes with lactoperoxidase, and digestion of whole cells and membranes with chymotrypsin, One of these proteins is synthesized as a precursor, and about 20-40 amino acids are removed after it is incorporated into the membrane, We discuss the probable sites of synthesis of these and other classes of membrane proteins. |
format | Text |
id | pubmed-2111166 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1975 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21111662008-05-01 Membrane proteins synthesized by rabbit reticulocytes J Cell Biol Articles Intact rabbit reticulocyte cells synthesize two predominant species of polypeptides which are components of the cell plasma membrane. Previous work (Lodish, H. F. 1973. Proc. Natl. Acad. Sci. U. S. A. 70:1526- 1530.) showed that these proteins were synthesized by polyribosomes not attached to membranes. We show here that both polypeptides are confined to the cytoplasmic surface of the cell membrane. These studies utilized iodination of whole cells and of membranes with lactoperoxidase, and digestion of whole cells and membranes with chymotrypsin, One of these proteins is synthesized as a precursor, and about 20-40 amino acids are removed after it is incorporated into the membrane, We discuss the probable sites of synthesis of these and other classes of membrane proteins. The Rockefeller University Press 1975-04-01 /pmc/articles/PMC2111166/ /pubmed/1127015 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 Membrane proteins synthesized by rabbit reticulocytes |
title | Membrane proteins synthesized by rabbit reticulocytes |
title_full | Membrane proteins synthesized by rabbit reticulocytes |
title_fullStr | Membrane proteins synthesized by rabbit reticulocytes |
title_full_unstemmed | Membrane proteins synthesized by rabbit reticulocytes |
title_short | Membrane proteins synthesized by rabbit reticulocytes |
title_sort | membrane proteins synthesized by rabbit reticulocytes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111166/ https://www.ncbi.nlm.nih.gov/pubmed/1127015 |