Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: McDougal, D. B., Schimke, Robert T., Jones, Elizabeth M., Touhill, Elizabeth
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1964
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195390/
https://www.ncbi.nlm.nih.gov/pubmed/14100962
_version_ 1782147834403880960
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
work_keys_str_mv AT mcdougaldb quantitativestudiesofwhitematteriienzymesinvolvedintriosephosphatemetabolism
AT schimkerobertt quantitativestudiesofwhitematteriienzymesinvolvedintriosephosphatemetabolism
AT joneselizabethm quantitativestudiesofwhitematteriienzymesinvolvedintriosephosphatemetabolism
AT touhillelizabeth quantitativestudiesofwhitematteriienzymesinvolvedintriosephosphatemetabolism