Fumarase From Ascaris Suum: Partial Purification and Characterization

One molecular form of fumarase from Ascaris suum was demonstrated by cellulose acetate electroporesis and isoelectric focusing. The enzyme was partially purified by ammonium sulfate fractionation and ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of th...

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Main Author: Powley, David G.
Format: Others
Language:English
Published: North Texas State University 1976
Subjects:
Online Access:https://digital.library.unt.edu/ark:/67531/metadc798110/
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spelling ndltd-unt.edu-info-ark-67531-metadc7981102020-11-11T05:31:27Z Fumarase From Ascaris Suum: Partial Purification and Characterization Powley, David G. Ascaris suum Biology fumarase Ascarididae. Fumarase. One molecular form of fumarase from Ascaris suum was demonstrated by cellulose acetate electroporesis and isoelectric focusing. The enzyme was partially purified by ammonium sulfate fractionation and ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of the partially purified by ammonium sulfate fractionation amd ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of the partially purified preparation showed glyceraldehyde-3-phosphate dehydrongenase to be the major preparative contaminant. North Texas State University 1976-05 Thesis or Dissertation 79 leaves : ill. Text local-cont-no: 1002773185-Powley call-no: 379 N81 no.5170 oclc: 2438765 untcat: b1154016 https://digital.library.unt.edu/ark:/67531/metadc798110/ ark: ark:/67531/metadc798110 English Public Powley, David G. Copyright Copyright is held by the author, unless otherwise noted. All rights
collection NDLTD
language English
format Others
sources NDLTD
topic Ascaris suum
Biology
fumarase
Ascarididae.
Fumarase.
spellingShingle Ascaris suum
Biology
fumarase
Ascarididae.
Fumarase.
Powley, David G.
Fumarase From Ascaris Suum: Partial Purification and Characterization
description One molecular form of fumarase from Ascaris suum was demonstrated by cellulose acetate electroporesis and isoelectric focusing. The enzyme was partially purified by ammonium sulfate fractionation and ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of the partially purified by ammonium sulfate fractionation amd ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of the partially purified preparation showed glyceraldehyde-3-phosphate dehydrongenase to be the major preparative contaminant.
author Powley, David G.
author_facet Powley, David G.
author_sort Powley, David G.
title Fumarase From Ascaris Suum: Partial Purification and Characterization
title_short Fumarase From Ascaris Suum: Partial Purification and Characterization
title_full Fumarase From Ascaris Suum: Partial Purification and Characterization
title_fullStr Fumarase From Ascaris Suum: Partial Purification and Characterization
title_full_unstemmed Fumarase From Ascaris Suum: Partial Purification and Characterization
title_sort fumarase from ascaris suum: partial purification and characterization
publisher North Texas State University
publishDate 1976
url https://digital.library.unt.edu/ark:/67531/metadc798110/
work_keys_str_mv AT powleydavidg fumarasefromascarissuumpartialpurificationandcharacterization
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