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Arginase and Glugose-6-Phosphate Dehydrogenase Activities in Spontaneous Mammary Carcinogenesis
Arginase and glucose-6-phosphate dehydrogenase activities in the mammary glands of 4, 8 and 12 month old groups and in precancerous nodules and mammary tumours in (C3H Jax) virgin mice were studied. It was observed that activities of both the enzymes in different age groups of both the strains are c...
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group
1971
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2008539/ https://www.ncbi.nlm.nih.gov/pubmed/5581293 |
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author | Bhide, S. V. |
author_facet | Bhide, S. V. |
author_sort | Bhide, S. V. |
collection | PubMed |
description | Arginase and glucose-6-phosphate dehydrogenase activities in the mammary glands of 4, 8 and 12 month old groups and in precancerous nodules and mammary tumours in (C3H Jax) virgin mice were studied. It was observed that activities of both the enzymes in different age groups of both the strains are comparable, but are significantly lower than those present in precancerous nodules and mammary tumour. Activities of both the enzymes in the precancerous nodules and tumour tissue are comparable. |
format | Text |
id | pubmed-2008539 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1971 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-20085392009-09-10 Arginase and Glugose-6-Phosphate Dehydrogenase Activities in Spontaneous Mammary Carcinogenesis Bhide, S. V. Br J Cancer Articles Arginase and glucose-6-phosphate dehydrogenase activities in the mammary glands of 4, 8 and 12 month old groups and in precancerous nodules and mammary tumours in (C3H Jax) virgin mice were studied. It was observed that activities of both the enzymes in different age groups of both the strains are comparable, but are significantly lower than those present in precancerous nodules and mammary tumour. Activities of both the enzymes in the precancerous nodules and tumour tissue are comparable. Nature Publishing Group 1971-03 /pmc/articles/PMC2008539/ /pubmed/5581293 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 | Articles Bhide, S. V. Arginase and Glugose-6-Phosphate Dehydrogenase Activities in Spontaneous Mammary Carcinogenesis |
title | Arginase and Glugose-6-Phosphate Dehydrogenase Activities in Spontaneous Mammary Carcinogenesis |
title_full | Arginase and Glugose-6-Phosphate Dehydrogenase Activities in Spontaneous Mammary Carcinogenesis |
title_fullStr | Arginase and Glugose-6-Phosphate Dehydrogenase Activities in Spontaneous Mammary Carcinogenesis |
title_full_unstemmed | Arginase and Glugose-6-Phosphate Dehydrogenase Activities in Spontaneous Mammary Carcinogenesis |
title_short | Arginase and Glugose-6-Phosphate Dehydrogenase Activities in Spontaneous Mammary Carcinogenesis |
title_sort | arginase and glugose-6-phosphate dehydrogenase activities in spontaneous mammary carcinogenesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2008539/ https://www.ncbi.nlm.nih.gov/pubmed/5581293 |
work_keys_str_mv | AT bhidesv arginaseandglugose6phosphatedehydrogenaseactivitiesinspontaneousmammarycarcinogenesis |