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Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas.
We have compared the levels of phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activities and the distribution of their isoenzymes in normal colon, liver and lung tissues, and in colon, liver and lung adenocarcinoma, lung squamous cell carcinoma and lung carcinoid. All tumou...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group
1997
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2222744/ https://www.ncbi.nlm.nih.gov/pubmed/9083331 |
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author | Durany, N. Joseph, J. Campo, E. Molina, R. Carreras, J. |
author_facet | Durany, N. Joseph, J. Campo, E. Molina, R. Carreras, J. |
author_sort | Durany, N. |
collection | PubMed |
description | We have compared the levels of phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activities and the distribution of their isoenzymes in normal colon, liver and lung tissues, and in colon, liver and lung adenocarcinoma, lung squamous cell carcinoma and lung carcinoid. All tumours presented higher phosphoglycerate mutase and enolase activities and lower 2,3-bisphosphoglycerate phosphatase activity than the normal tissues. No changes were observed in the phosphoglycerate mutase isoenzyme patterns analysed by cellulose acetate electrophoresis. All specimens contained mainly type BB isoenzyme, traces of type MB isoenzyme and no type MM isoenzyme. However, the tumours had decreased levels of 2,3-bisphosphoglycerate mutase and 2,3-bisphosphoglycerate mutase-phosphoglycerate mutase hybrid enzyme. Determined by agarose gel electrophoresis, alpha alpha-enolase was the isoenzyme predominant in normal lung, colon and liver tissue, although alpha gamma- and gamma gamma-enolase were also present in all tissues. In colon, liver and non-endocrine lung tumours, the proportions of alpha gamma- and gamma gamma-enolase decreased. In contrast, in carcinoid tumours of the lung, the proportions of these isoenzymes increased. IMAGES: |
format | Text |
id | pubmed-2222744 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1997 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-22227442009-09-10 Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. Durany, N. Joseph, J. Campo, E. Molina, R. Carreras, J. Br J Cancer Research Article We have compared the levels of phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activities and the distribution of their isoenzymes in normal colon, liver and lung tissues, and in colon, liver and lung adenocarcinoma, lung squamous cell carcinoma and lung carcinoid. All tumours presented higher phosphoglycerate mutase and enolase activities and lower 2,3-bisphosphoglycerate phosphatase activity than the normal tissues. No changes were observed in the phosphoglycerate mutase isoenzyme patterns analysed by cellulose acetate electrophoresis. All specimens contained mainly type BB isoenzyme, traces of type MB isoenzyme and no type MM isoenzyme. However, the tumours had decreased levels of 2,3-bisphosphoglycerate mutase and 2,3-bisphosphoglycerate mutase-phosphoglycerate mutase hybrid enzyme. Determined by agarose gel electrophoresis, alpha alpha-enolase was the isoenzyme predominant in normal lung, colon and liver tissue, although alpha gamma- and gamma gamma-enolase were also present in all tissues. In colon, liver and non-endocrine lung tumours, the proportions of alpha gamma- and gamma gamma-enolase decreased. In contrast, in carcinoid tumours of the lung, the proportions of these isoenzymes increased. IMAGES: Nature Publishing Group 1997 /pmc/articles/PMC2222744/ /pubmed/9083331 Text en https://creativecommons.org/licenses/by/4.0/This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Research Article Durany, N. Joseph, J. Campo, E. Molina, R. Carreras, J. Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. |
title | Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. |
title_full | Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. |
title_fullStr | Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. |
title_full_unstemmed | Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. |
title_short | Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. |
title_sort | phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas. |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2222744/ https://www.ncbi.nlm.nih.gov/pubmed/9083331 |
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