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Quantitative Studies of White Matter : II. Enzymes involved in triose phosphate metabolism
Methods for measurement of glyceraldehyde-P dehydrogenase, triose-P isomerase, fructose 1,6-diphosphate aldolase, and the DPN-linked and flavin-linked α-glycero-P dehydrogenases in small amounts of tissue have been worked out. These enzymes have been measured in ten tracts in rabbit central nervous...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1964
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195390/ https://www.ncbi.nlm.nih.gov/pubmed/14100962 |
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author | McDougal, D. B. Schimke, Robert T. Jones, Elizabeth M. Touhill, Elizabeth |
author_facet | McDougal, D. B. Schimke, Robert T. Jones, Elizabeth M. Touhill, Elizabeth |
author_sort | McDougal, D. B. |
collection | PubMed |
description | Methods for measurement of glyceraldehyde-P dehydrogenase, triose-P isomerase, fructose 1,6-diphosphate aldolase, and the DPN-linked and flavin-linked α-glycero-P dehydrogenases in small amounts of tissue have been worked out. These enzymes have been measured in ten tracts in rabbit central nervous system. The activities of all the enzymes measured, except the flavin-linked α-glycero-P dehydrogenase, are present in larger amounts in lightly myelinated than in heavily myelinated tracts, but are relatively low in fibrillar layer of olfactory bulb, which is unmyelinated. Aldolase, like P-fructokinase (measured previously), is especially low in fibrillar layer. Taken together with relatively high 6-P-gluconate dehydrogenase activity found earlier this supports the hypothesis that the pentose-P shunt is particularly active in this tract. The activity of DPN-linked α-glycero-P dehydrogenase is inversely proportional to the lipid content of the myelinated tracts, which suggests that its primary role is not related to lipid synthesis in adult brain. The activities of flavin-linked α-glycero-P dehydrogenase are unrelated to those of the DPN-linked enzyme, which is contrary to expectation if the two enzymes function as partners in the "α-glycerophosphate shuttle." |
format | Text |
id | pubmed-2195390 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1964 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21953902008-04-23 Quantitative Studies of White Matter : II. Enzymes involved in triose phosphate metabolism McDougal, D. B. Schimke, Robert T. Jones, Elizabeth M. Touhill, Elizabeth J Gen Physiol Article Methods for measurement of glyceraldehyde-P dehydrogenase, triose-P isomerase, fructose 1,6-diphosphate aldolase, and the DPN-linked and flavin-linked α-glycero-P dehydrogenases in small amounts of tissue have been worked out. These enzymes have been measured in ten tracts in rabbit central nervous system. The activities of all the enzymes measured, except the flavin-linked α-glycero-P dehydrogenase, are present in larger amounts in lightly myelinated than in heavily myelinated tracts, but are relatively low in fibrillar layer of olfactory bulb, which is unmyelinated. Aldolase, like P-fructokinase (measured previously), is especially low in fibrillar layer. Taken together with relatively high 6-P-gluconate dehydrogenase activity found earlier this supports the hypothesis that the pentose-P shunt is particularly active in this tract. The activity of DPN-linked α-glycero-P dehydrogenase is inversely proportional to the lipid content of the myelinated tracts, which suggests that its primary role is not related to lipid synthesis in adult brain. The activities of flavin-linked α-glycero-P dehydrogenase are unrelated to those of the DPN-linked enzyme, which is contrary to expectation if the two enzymes function as partners in the "α-glycerophosphate shuttle." The Rockefeller University Press 1964-01-01 /pmc/articles/PMC2195390/ /pubmed/14100962 Text en Copyright ©, 1964, by The Rockefeller Institute Press 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 | Article McDougal, D. B. Schimke, Robert T. Jones, Elizabeth M. Touhill, Elizabeth Quantitative Studies of White Matter : II. Enzymes involved in triose phosphate metabolism |
title | Quantitative Studies of White Matter : II. Enzymes involved in triose phosphate metabolism |
title_full | Quantitative Studies of White Matter : II. Enzymes involved in triose phosphate metabolism |
title_fullStr | Quantitative Studies of White Matter : II. Enzymes involved in triose phosphate metabolism |
title_full_unstemmed | Quantitative Studies of White Matter : II. Enzymes involved in triose phosphate metabolism |
title_short | Quantitative Studies of White Matter : II. Enzymes involved in triose phosphate metabolism |
title_sort | quantitative studies of white matter : ii. enzymes involved in triose phosphate metabolism |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195390/ https://www.ncbi.nlm.nih.gov/pubmed/14100962 |
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