Cargando…
Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid)
Specific antibodies against human alpha1-acid glycoprotein reacted with human lymphocytes, granulocytes, and monocytes. The antigen on the leukocytes is an externally located integral membrane glycoprotein which is made by the cells and has an apparent mol wt of 52,000. It is released from cells in...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1978
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2184935/ https://www.ncbi.nlm.nih.gov/pubmed/702047 |
_version_ | 1782145725541384192 |
---|---|
collection | PubMed |
description | Specific antibodies against human alpha1-acid glycoprotein reacted with human lymphocytes, granulocytes, and monocytes. The antigen on the leukocytes is an externally located integral membrane glycoprotein which is made by the cells and has an apparent mol wt of 52,000. It is released from cells in vitro to the culture medium. The mol wt of the soluble fragment is 41,000, which corresponds to that of alpha1-acid glycoprotein in serum and urine. Peptide mapping confirmed that the main part of the cellular membrane antigen consists of alpha1-acid glycoprotein with an additional, probably hydrophobic fragment. This finding may partially explain the increase in the serum levels of alpha1-acid glycoprotein observed in many disorders involving leukocyte proliferation. In addition, the known sequence homology of alpha1-acid glycoprotein with immunoglobulins can now be more easily understood by their origin in similar cell types. |
format | Text |
id | pubmed-2184935 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1978 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21849352008-04-17 Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid) J Exp Med Articles Specific antibodies against human alpha1-acid glycoprotein reacted with human lymphocytes, granulocytes, and monocytes. The antigen on the leukocytes is an externally located integral membrane glycoprotein which is made by the cells and has an apparent mol wt of 52,000. It is released from cells in vitro to the culture medium. The mol wt of the soluble fragment is 41,000, which corresponds to that of alpha1-acid glycoprotein in serum and urine. Peptide mapping confirmed that the main part of the cellular membrane antigen consists of alpha1-acid glycoprotein with an additional, probably hydrophobic fragment. This finding may partially explain the increase in the serum levels of alpha1-acid glycoprotein observed in many disorders involving leukocyte proliferation. In addition, the known sequence homology of alpha1-acid glycoprotein with immunoglobulins can now be more easily understood by their origin in similar cell types. The Rockefeller University Press 1978-08-01 /pmc/articles/PMC2184935/ /pubmed/702047 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 Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid) |
title | Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid) |
title_full | Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid) |
title_fullStr | Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid) |
title_full_unstemmed | Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid) |
title_short | Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid) |
title_sort | leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid) |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2184935/ https://www.ncbi.nlm.nih.gov/pubmed/702047 |