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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1976
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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 |
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English |
format |
Others
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Ascaris suum Biology fumarase Ascarididae. Fumarase. |
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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 |
_version_ |
1719356101110005760 |