Isolation and characterization of Glyceraldehyde-3-phosphate dehydrogenase from the common octopus (Octopus vulgaris Cuvier, 1797)
The NAD⁺ dependent cytosolic Glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) from arms of Octopus vulgaris, Cuvier, 1787, (Octopoda, Cephalopoda) was purified to homogeneity and its kinetic properties investigated. The purification method consisted of ammonium sulfate fractionation fol...
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| Veröffentlicht in: | Reviews in fish biology and fisheries 2008-08, Vol.18 (3), p.263-271 |
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| creator | Oukhattar, Laila Baibai, Tarik Moutaouakkil, Adnane Assobhei, Omar Soukri, Abdelaziz |
| description | The NAD⁺ dependent cytosolic Glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) from arms of Octopus vulgaris, Cuvier, 1787, (Octopoda, Cephalopoda) was purified to homogeneity and its kinetic properties investigated. The purification method consisted of ammonium sulfate fractionation followed by Blue Sepharose CL-6B chromatography resulting in a 26-fold increase in specific activity and a final yield of approximately 16%. The apparent molecular weight of the purified native enzyme was 153 kDa. The protein is an homotetramer, composed of identical subunits with an apparent molecular weight of approximately 36 kDa. The Michaelis constants Km for both NAD⁺ and d-G3P were 66 μM and 320 μM, respectively. The maximal velocity Vmax of the purified enzyme was estimated to be 21.8 U/mg. Only one GAPDH isoform (pI 6.6) was obtained by isoelectrofocusing in polyacrylamide slab gels holding ampholyte generated pH gradients. Under the conditions of assay, the optimum activity occurs at pH 7.0 and at temperature of 35°C. Polyclonal antibodies raised in rabbits against the purified GAPDH immunostained a single 36 kDa GAPDH band on crude extract protein preparations blotted onto nitrocellulose. |
| doi_str_mv | 10.1007/s11160-007-9074-6 |
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The purification method consisted of ammonium sulfate fractionation followed by Blue Sepharose CL-6B chromatography resulting in a 26-fold increase in specific activity and a final yield of approximately 16%. The apparent molecular weight of the purified native enzyme was 153 kDa. The protein is an homotetramer, composed of identical subunits with an apparent molecular weight of approximately 36 kDa. The Michaelis constants Km for both NAD⁺ and d-G3P were 66 μM and 320 μM, respectively. The maximal velocity Vmax of the purified enzyme was estimated to be 21.8 U/mg. Only one GAPDH isoform (pI 6.6) was obtained by isoelectrofocusing in polyacrylamide slab gels holding ampholyte generated pH gradients. Under the conditions of assay, the optimum activity occurs at pH 7.0 and at temperature of 35°C. Polyclonal antibodies raised in rabbits against the purified GAPDH immunostained a single 36 kDa GAPDH band on crude extract protein preparations blotted onto nitrocellulose.</description><identifier>ISSN: 0960-3166</identifier><identifier>EISSN: 1573-5184</identifier><identifier>DOI: 10.1007/s11160-007-9074-6</identifier><language>eng</language><publisher>Dordrecht: Dordrecht : Springer Netherlands</publisher><subject>Ammonium ; Biomedical and Life Sciences ; Cephalopoda ; Characterization ; Chromatography ; Dehydrogenase ; Dehydrogenases ; Enzyme kinetics ; Enzymes ; Fisheries ; Fractionation ; Freshwater & Marine Ecology ; glyceraldehyde-3-phosphate dehydrogenase ; Glycerol ; Kinetics ; Life Sciences ; Marine ; Marine biology ; Molecular weight ; Octopoda ; Octopus vulgaris ; Proteins ; purification ; Research Paper ; Studies ; Zoology</subject><ispartof>Reviews in fish biology and fisheries, 2008-08, Vol.18 (3), p.263-271</ispartof><rights>Springer Science+Business Media B.V. 2007</rights><rights>Springer Science+Business Media B.V. 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c371t-1de866dc1c8bb94dc713a8ed60a41d848da833d0e056b91988444a05344e5de93</citedby><cites>FETCH-LOGICAL-c371t-1de866dc1c8bb94dc713a8ed60a41d848da833d0e056b91988444a05344e5de93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11160-007-9074-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11160-007-9074-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Oukhattar, Laila</creatorcontrib><creatorcontrib>Baibai, Tarik</creatorcontrib><creatorcontrib>Moutaouakkil, Adnane</creatorcontrib><creatorcontrib>Assobhei, Omar</creatorcontrib><creatorcontrib>Soukri, Abdelaziz</creatorcontrib><title>Isolation and characterization of Glyceraldehyde-3-phosphate dehydrogenase from the common octopus (Octopus vulgaris Cuvier, 1797)</title><title>Reviews in fish biology and fisheries</title><addtitle>Rev Fish Biol Fisheries</addtitle><description>The NAD⁺ dependent cytosolic Glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) from arms of Octopus vulgaris, Cuvier, 1787, (Octopoda, Cephalopoda) was purified to homogeneity and its kinetic properties investigated. The purification method consisted of ammonium sulfate fractionation followed by Blue Sepharose CL-6B chromatography resulting in a 26-fold increase in specific activity and a final yield of approximately 16%. The apparent molecular weight of the purified native enzyme was 153 kDa. The protein is an homotetramer, composed of identical subunits with an apparent molecular weight of approximately 36 kDa. The Michaelis constants Km for both NAD⁺ and d-G3P were 66 μM and 320 μM, respectively. The maximal velocity Vmax of the purified enzyme was estimated to be 21.8 U/mg. Only one GAPDH isoform (pI 6.6) was obtained by isoelectrofocusing in polyacrylamide slab gels holding ampholyte generated pH gradients. Under the conditions of assay, the optimum activity occurs at pH 7.0 and at temperature of 35°C. Polyclonal antibodies raised in rabbits against the purified GAPDH immunostained a single 36 kDa GAPDH band on crude extract protein preparations blotted onto nitrocellulose.</description><subject>Ammonium</subject><subject>Biomedical and Life Sciences</subject><subject>Cephalopoda</subject><subject>Characterization</subject><subject>Chromatography</subject><subject>Dehydrogenase</subject><subject>Dehydrogenases</subject><subject>Enzyme kinetics</subject><subject>Enzymes</subject><subject>Fisheries</subject><subject>Fractionation</subject><subject>Freshwater & Marine Ecology</subject><subject>glyceraldehyde-3-phosphate dehydrogenase</subject><subject>Glycerol</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Marine</subject><subject>Marine biology</subject><subject>Molecular weight</subject><subject>Octopoda</subject><subject>Octopus vulgaris</subject><subject>Proteins</subject><subject>purification</subject><subject>Research 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Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oukhattar, Laila</au><au>Baibai, Tarik</au><au>Moutaouakkil, Adnane</au><au>Assobhei, Omar</au><au>Soukri, Abdelaziz</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of Glyceraldehyde-3-phosphate dehydrogenase from the common octopus (Octopus vulgaris Cuvier, 1797)</atitle><jtitle>Reviews in fish biology and fisheries</jtitle><stitle>Rev Fish Biol Fisheries</stitle><date>2008-08-01</date><risdate>2008</risdate><volume>18</volume><issue>3</issue><spage>263</spage><epage>271</epage><pages>263-271</pages><issn>0960-3166</issn><eissn>1573-5184</eissn><abstract>The NAD⁺ dependent cytosolic Glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) from arms of Octopus vulgaris, Cuvier, 1787, (Octopoda, Cephalopoda) was purified to homogeneity and its kinetic properties investigated. The purification method consisted of ammonium sulfate fractionation followed by Blue Sepharose CL-6B chromatography resulting in a 26-fold increase in specific activity and a final yield of approximately 16%. The apparent molecular weight of the purified native enzyme was 153 kDa. The protein is an homotetramer, composed of identical subunits with an apparent molecular weight of approximately 36 kDa. The Michaelis constants Km for both NAD⁺ and d-G3P were 66 μM and 320 μM, respectively. The maximal velocity Vmax of the purified enzyme was estimated to be 21.8 U/mg. Only one GAPDH isoform (pI 6.6) was obtained by isoelectrofocusing in polyacrylamide slab gels holding ampholyte generated pH gradients. Under the conditions of assay, the optimum activity occurs at pH 7.0 and at temperature of 35°C. Polyclonal antibodies raised in rabbits against the purified GAPDH immunostained a single 36 kDa GAPDH band on crude extract protein preparations blotted onto nitrocellulose.</abstract><cop>Dordrecht</cop><pub>Dordrecht : Springer Netherlands</pub><doi>10.1007/s11160-007-9074-6</doi><tpages>9</tpages></addata></record> |
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| subjects | Ammonium Biomedical and Life Sciences Cephalopoda Characterization Chromatography Dehydrogenase Dehydrogenases Enzyme kinetics Enzymes Fisheries Fractionation Freshwater & Marine Ecology glyceraldehyde-3-phosphate dehydrogenase Glycerol Kinetics Life Sciences Marine Marine biology Molecular weight Octopoda Octopus vulgaris Proteins purification Research Paper Studies Zoology |
| title | Isolation and characterization of Glyceraldehyde-3-phosphate dehydrogenase from the common octopus (Octopus vulgaris Cuvier, 1797) |
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